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. 1976 Apr 1;69(1):173–195. doi: 10.1083/jcb.69.1.173

Involvement of vesicle coat material in casein secretion and surface regeneration

PMCID: PMC2110961  PMID: 1254641

Abstract

The ultrastructure of the apical zone of lactating rat mammary epithelial cells was studied with emphasis on vesicle coat structures. Typical 40-60 nm ID "coated vesicles" were abundant, frequently associated with the internal filamentous plasma membrane coat or in direct continuity with secretory vesicles (SV) or plasma membrane proper. Bristle coats partially or totally covered membranes of secretory vesicles identified by their casein micelle content. This coat survived SV isolation. Exocytotic fusion of SV membranes and release of the casein micelles was observed. Frequently, regularly arranged bristle coat structures were identified in those regions of the plasma membrane that were involved in exocytotic processes. Both coated and uncoated surfaces of the casein-containing vesicles, as well as typical "coated vesicles", were frequently associated with microtubules and/or microfilaments. We suggest that coat materials of vesicles are related or identical to components of the internal coat of the surface membrane and that new plasma membrane and associated internal coat is produced concomitantly by fusion and integration of bristle coat moieties. Postexocytotic association of secreted casein micelles with the cell surface, mediated by finely filamentous extensions, provided a marker for the integrated vesicle membrane. An arrangement of SV with the inner surface of the plasma membrane is described which is characterized by regularly spaced, heabily stained membrane to membrane cross-bridges (pre-exocytotic attachment plaques). Such membrane-interconnecting elements may represent a form of coat structure important to recognition and interaction of membrane surfaces.

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Selected References

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  1. Allen R. D. Evidence for firm linkages between microtubules and membrane-bounded vesicles. J Cell Biol. 1975 Feb;64(2):497–503. doi: 10.1083/jcb.64.2.497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Allen R. D. Structures linking the myonemes, endoplasmic reticulum, and surface membranes in the contractile ciliate Vorticella. J Cell Biol. 1973 Feb;56(2):559–579. doi: 10.1083/jcb.56.2.559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Amsterdam A., Ohad I., Schramm M. Dynamic changes in the ultrastructure of the acinar cell of the rat parotid gland during the secretory cycle. J Cell Biol. 1969 Jun;41(3):753–773. doi: 10.1083/jcb.41.3.753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Amsterdam A., Schramm M., Ohad I., Salomon Y., Selinger Z. Concomitant synthesis of membrane protein and exportable protein of the secretory granule in rat parotid gland. J Cell Biol. 1971 Jul;50(1):187–200. doi: 10.1083/jcb.50.1.187. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Anderson W. A., Trantalis J., Kang Y. H. Ultrastructural localization of endogenous mammary gland peroxidase during lactogenesis in the rat results after tannic acid-formaldehyde-glutaraldehyde fixation. J Histochem Cytochem. 1975 Apr;23(4):295–302. doi: 10.1177/23.4.47872. [DOI] [PubMed] [Google Scholar]
  6. BARGMANN W., FLEISCHHAUTER K., KNOOP A. [On the morphology of milk secretion. II. With a criticism of the scheme of secretion morphology]. Z Zellforsch Mikrosk Anat. 1961;53:545–568. [PubMed] [Google Scholar]
  7. BARGMANN W., KNOOP A. Uber die Morphologie der Milchsekretion; lichtund elektronenmikroskopische Studien an der Milchdrüse Ratte. Z Zellforsch Mikrosk Anat. 1959;49(3):344–388. [PubMed] [Google Scholar]
  8. Bardele C. F. A microtubule model for ingestion and transport in the suctorian tentacle. Z Zellforsch Mikrosk Anat. 1972;126(1):116–134. doi: 10.1007/BF00306784. [DOI] [PubMed] [Google Scholar]
  9. Bauer H. Ultrastructural observations on the milk fat globule envelope of cow's milk. J Dairy Sci. 1972 Oct;55(10):1375–1387. doi: 10.3168/jds.S0022-0302(72)85680-7. [DOI] [PubMed] [Google Scholar]
  10. Baumrucker C. R., Keenan T. W. Membranes of mammary gland. X. Adenosine triphosphate dependent calcium accumulation by Golgi apparatus rich fractions from bovine mammary gland. Exp Cell Res. 1975 Feb;90(2):253–260. doi: 10.1016/0014-4827(75)90314-6. [DOI] [PubMed] [Google Scholar]
  11. Beery K. E., Hood L. F., Patton S. Formation of casein micelles in golgi vesicles of mammary tissue. J Dairy Sci. 1971 Jun;54(6):911–912. doi: 10.3168/jds.S0022-0302(71)85940-4. [DOI] [PubMed] [Google Scholar]
  12. Bergeron J. J., Evans W. H., Geschwind I. I. Insulin binding to rat liver Golgi fractions. J Cell Biol. 1973 Dec;59(3):771–776. doi: 10.1083/jcb.59.3.771. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Berl S., Puszkin S., Nicklas W. J. Actomyosin-like protein in brain. Science. 1973 Feb 2;179(4072):441–446. doi: 10.1126/science.179.4072.441. [DOI] [PubMed] [Google Scholar]
  14. Blitz A. L., Fine R. E. Muscle-like contractile proteins and tubulin in synaptosomes. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4472–4476. doi: 10.1073/pnas.71.11.4472. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Bluemink J. G. Cortical wound healing in the amphibian egg: an electron microscopical study. J Ultrastruct Res. 1972 Oct;41(1):95–114. doi: 10.1016/s0022-5320(72)90041-x. [DOI] [PubMed] [Google Scholar]
  16. Bousquet M., Fléchon J. E., Denamur R. Aspects ultrastructuraux de la glande mammaire de lapine pendant la lactogénèse. Z Zellforsch Mikrosk Anat. 1969;96(3):418–436. [PubMed] [Google Scholar]
  17. Brew K. Secretion of alpha-lactalbumin into milk and its relevance to the organization and control of lactose synthetase. Nature. 1969 May 17;222(5194):671–672. doi: 10.1038/222671a0. [DOI] [PubMed] [Google Scholar]
  18. Bruni C., Porter K. R. The Fine Structure of the Parenchymal Cell of the Normal Rat Liver: I. General Observations. Am J Pathol. 1965 May;46(5):691–755. [PMC free article] [PubMed] [Google Scholar]
  19. Bruns R. R., Palade G. E. Studies on blood capillaries. I. General organization of blood capillaries in muscle. J Cell Biol. 1968 May;37(2):244–276. doi: 10.1083/jcb.37.2.244. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Burridge K., Phillips J. H. Association of actin and myosin with secretory granule membranes. Nature. 1975 Apr 10;254(5500):526–529. doi: 10.1038/254526a0. [DOI] [PubMed] [Google Scholar]
  21. Choi Y. S., Knopf P. M., Lennox E. S. Intracellular transport and secretion of an immunoglobulin light chain. Biochemistry. 1971 Feb 16;10(4):668–679. doi: 10.1021/bi00780a019. [DOI] [PubMed] [Google Scholar]
  22. Clarke M., Schatten G., Mazia D., Spudich J. A. Visualization of actin fibers associated with the cell membrane in amoebae of Dictyostelium discoideum. Proc Natl Acad Sci U S A. 1975 May;72(5):1758–1762. doi: 10.1073/pnas.72.5.1758. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Comly L. T. Microfilaments in Chaos carolinensis. Membrane association, distribution, and heavy meromyosin binding in the glycerinated cell. J Cell Biol. 1973 Jul;58(1):230–237. doi: 10.1083/jcb.58.1.230. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Cronshaw J., Esau K. Cell division in leaves of Nicotiana. Protoplasma. 1968;65(1):1–24. doi: 10.1007/BF01666368. [DOI] [PubMed] [Google Scholar]
  25. Danneel S., Weissenfels N. Besseres Fixierungsverfahren zur Darstellung des Grundplasmas von Protozoen und Vertebratenzellen. Mikroskopie. 1965 Oct;20(3):89–93. [PubMed] [Google Scholar]
  26. Dewan R. K., Chudgar A., Mead R., Bloomfield V. A., Morr C. V. Molecular weight and size distribution of bovine milk casein micelles. Biochim Biophys Acta. 1974 Apr 11;342(2):313–321. doi: 10.1016/0005-2795(74)90086-5. [DOI] [PubMed] [Google Scholar]
  27. Droller M. J., Roth T. F. An electron microscope study of yolk formation during oogenesis in Lebistes reticulatus guppyi. J Cell Biol. 1966 Feb;28(2):209–232. doi: 10.1083/jcb.28.2.209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Dumont A. Ultrastructural study of the maturation of peritoneal macrophages in the hamster. J Ultrastruct Res. 1969 Nov;29(3):191–209. doi: 10.1016/s0022-5320(69)90100-2. [DOI] [PubMed] [Google Scholar]
  29. Durham A. C. A unified theory of the control of actin and myosin in nonmuscle movements. Cell. 1974 Jul;2(3):123–135. doi: 10.1016/0092-8674(74)90087-7. [DOI] [PubMed] [Google Scholar]
  30. ERICSSON J. L. TRANSPORT AND DIGESTION OF HEMOGLOBIN IN THE PROXIMAL TUBULE. II. ELECTRON MICROSCOPY. Lab Invest. 1965 Jan;14:16–39. [PubMed] [Google Scholar]
  31. Ehrlich H. P., Bornstein P. Microtubules in transcellular movement of procollagen. Nat New Biol. 1972 Aug 30;238(87):257–260. doi: 10.1038/newbio238257a0. [DOI] [PubMed] [Google Scholar]
  32. FAWCETT D. W. SURFACE SPECIALIZATIONS OF ABSORBING CELLS. J Histochem Cytochem. 1965 Feb;13:75–91. doi: 10.1177/13.2.75. [DOI] [PubMed] [Google Scholar]
  33. FELDMAN J. D. Fine structure of the cow's udder during gestation and lactation. Lab Invest. 1961 Mar-Apr;10:238–255. [PubMed] [Google Scholar]
  34. Faulk W. P., Conochie L. B., Temple A., Papamichail M. Immunobiology of membrane-bound collagen on mouse fibroblasts. Nature. 1975 Jul 10;256(5513):123–125. doi: 10.1038/256123a0. [DOI] [PubMed] [Google Scholar]
  35. Franke W. W. Cytoplasmic microtubules linked to endoplasmic reticulum with cross-bridges. Exp Cell Res. 1971 Jun;66(2):486–489. doi: 10.1016/0014-4827(71)90705-1. [DOI] [PubMed] [Google Scholar]
  36. Franke W. W., Deumling B., Baerbelermen, Jarasch E. D., Kleinig H. Nuclear membranes from mammalian liver. I. Isolation procedure and general characterization. J Cell Biol. 1970 Aug;46(2):379–395. doi: 10.1083/jcb.46.2.379. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Franke W. W., Herth W. Morphological evidence for de novo formation of plasma membrane from coated vesicles in exponentially growing cultured plant cells. Exp Cell Res. 1974 Dec;89(2):447–451. doi: 10.1016/0014-4827(74)90821-0. [DOI] [PubMed] [Google Scholar]
  38. Franke W. W., Kartenbeck J., Krien S., VanderWoude W. J., Scheer U., Morré D. J. Inter- and intracisternal elements of the Golgi apparatus. A system of membrane-to-membrane cross-links. Z Zellforsch Mikrosk Anat. 1972;132(3):365–380. doi: 10.1007/BF02450714. [DOI] [PubMed] [Google Scholar]
  39. Franke W. W., Kartenbeck J., Zentgraf H., Scheer U., Falk H. Membrane-to-membrane cross-bridges. A means to orientation and interaction of membrane faces. J Cell Biol. 1971 Dec;51(3):881–888. doi: 10.1083/jcb.51.3.881. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Franke W. W., Krien S., Brown R. M., Jr Simultaneous glutaraldehyde-osmium tetroxide fixation with postosmication. An improved fixation procedure for electron microscopy of plant and animal cells. Histochemie. 1969;19(2):162–164. doi: 10.1007/BF00281096. [DOI] [PubMed] [Google Scholar]
  41. Franke W. W., Morré D. J., Deumling B., Cheetham R. D., Kartenbeck J., Jarasch E. D., Zentgraf H. W. Synthesis and turnover of membrane proteins in rat liver: an examination of the membrane flow hypothesis. Z Naturforsch B. 1971 Oct;26(10):1031–1039. doi: 10.1515/znb-1971-1016. [DOI] [PubMed] [Google Scholar]
  42. Franke W. W. On the universality of nuclear pore complex structure. Z Zellforsch Mikrosk Anat. 1970;105(3):405–429. doi: 10.1007/BF00335464. [DOI] [PubMed] [Google Scholar]
  43. Friend D. S., Farquhar M. G. Functions of coated vesicles during protein absorption in the rat vas deferens. J Cell Biol. 1967 Nov;35(2):357–376. doi: 10.1083/jcb.35.2.357. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. GRAY E. G. The granule cells, mossy synapses and Purkinje spine synapses of the cerebellum: light and electron microscope observations. J Anat. 1961 Jul;95:345–356. [PMC free article] [PubMed] [Google Scholar]
  45. Girardie J. Histo-cytomorphologie de la glande mammaire de la souris C3H et de trois autres rongeurs. Z Zellforsch Mikrosk Anat. 1968 Apr 25;87(4):478–503. [PubMed] [Google Scholar]
  46. Graham R. C., Jr, Karnovsky M. J. The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique. J Histochem Cytochem. 1966 Apr;14(4):291–302. doi: 10.1177/14.4.291. [DOI] [PubMed] [Google Scholar]
  47. Gray E. G. Are the coats of coated vesicles artefacts? J Neurocytol. 1972 Dec;1(4):363–382. doi: 10.1007/BF01102940. [DOI] [PubMed] [Google Scholar]
  48. Gray E. G. Synaptic fine structure and nuclear, cytoplasmic and extracellular networks: The stereoframework concept. J Neurocytol. 1975 Jun;4(3):315–339. doi: 10.1007/BF01102116. [DOI] [PubMed] [Google Scholar]
  49. Gray E. G. The cytonet, plain and coated vesicles, reticulosomes, multivesicular bodies and nuclear pores. Brain Res. 1973 Nov 23;62(2):329–335. doi: 10.1016/0006-8993(73)90693-8. [DOI] [PubMed] [Google Scholar]
  50. Gruenstein E., Rich A., Weihing R. R. Actin associated with membranes from 3T3 mouse fibroblast and HeLa cells. J Cell Biol. 1975 Jan;64(1):223–234. doi: 10.1083/jcb.64.1.223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Gwynn I., Kemp R. B., Jones B. M., Gröschel-Stewart U. Ultrastructural evidence for myosin of the smooth muscle type at the surface of trypsin-dissociated embryonic chick cells. J Cell Sci. 1974 Jul;15(2):279–289. doi: 10.1242/jcs.15.2.279. [DOI] [PubMed] [Google Scholar]
  52. Haustein D., Marchalonis J. J., Crumpton M. J. Immunoglobulin of T lymphoma cells is an integral membrane protein. Nature. 1974 Dec 13;252(5484):602–604. doi: 10.1038/252602a0. [DOI] [PubMed] [Google Scholar]
  53. Heald C. W. Hormonal effects on mammary cytology. J Dairy Sci. 1974 Aug;57(8):917–925. doi: 10.3168/jds.S0022-0302(74)84987-8. [DOI] [PubMed] [Google Scholar]
  54. Heald C. W., Saacke R. G. Cytological comparison of milk protein synthesis of rat mammary tissue in vivo and in vitro. J Dairy Sci. 1972 May;55(5):621–628. doi: 10.3168/jds.S0022-0302(72)85545-0. [DOI] [PubMed] [Google Scholar]
  55. Helminen H. J., Ericsson J. L. Studies on mammary gland involution. I. On the ultrastructure of the lactating mammary gland. J Ultrastruct Res. 1968 Nov;25(3):193–213. doi: 10.1016/s0022-5320(68)80069-3. [DOI] [PubMed] [Google Scholar]
  56. Hepler P. K., Newcomb E. H. Fine structure of cell plate formation in the apical meristem of Phaseolus roots. J Ultrastruct Res. 1967 Aug 30;19(5):498–513. doi: 10.1016/s0022-5320(67)80076-5. [DOI] [PubMed] [Google Scholar]
  57. Heuser J. E., Reese T. S. Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction. J Cell Biol. 1973 May;57(2):315–344. doi: 10.1083/jcb.57.2.315. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Hirano H., Parkhouse B., Nicolson G. L., Lennox E. S., Singer S. J. Distribution of saccharide residues on membrane fragments from a myeloma-cell homogenate: its implications for membrane biogenesis. Proc Natl Acad Sci U S A. 1972 Oct;69(10):2945–2949. doi: 10.1073/pnas.69.10.2945. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Hirsch J. G., Fedorko M. E. Ultrastructure of human leukocytes after simultaneous fixation with glutaraldehyde and osmium tetroxide and "postfixation" in uranyl acetate. J Cell Biol. 1968 Sep;38(3):615–627. doi: 10.1083/jcb.38.3.615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Hollmann K. H. Sur des aspects particuliers des protéines élaborées dans la glande mammaire. Etude au microscope électronique chez la lapine en lactation. Z Zellforsch Mikrosk Anat. 1966;69:395–402. [PubMed] [Google Scholar]
  61. Hopwood D. The reactions between formaldehyde, glutaraldehyde and osmium tetroxide, and their fixation effects o bovine serum albumin and on tissue blocks. Histochemie. 1970;24(1):50–64. doi: 10.1007/BF00310003. [DOI] [PubMed] [Google Scholar]
  62. Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex. J Cell Biol. 1967 Aug;34(2):577–596. doi: 10.1083/jcb.34.2.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Kanaseki T., Kadota K. The "vesicle in a basket". A morphological study of the coated vesicle isolated from the nerve endings of the guinea pig brain, with special reference to the mechanism of membrane movements. J Cell Biol. 1969 Jul;42(1):202–220. doi: 10.1083/jcb.42.1.202. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Kawasaki T., Yamashina I. Metabolic studies of rat liver plasma membranes using D-(1-14C)glucosamine. Biochim Biophys Acta. 1971 Feb 2;225(2):234–238. doi: 10.1016/0005-2736(71)90216-1. [DOI] [PubMed] [Google Scholar]
  65. Keenan T. W., Huang C. M. Membranes of mammary gland. VI. Lipid and protein composition of Golgi apparatus and rough endoplasmic reticulum from bovine mammary gland. J Dairy Sci. 1972 Nov;55(11):1586–1596. doi: 10.3168/jds.S0022-0302(72)85725-4. [DOI] [PubMed] [Google Scholar]
  66. Keenan T. W., Huang C. M., Morre D. J. Membranes of mammary gland. 3. Lipid composition of Golgi apparatus from rat mammary gland. J Dairy Sci. 1972 Jan;55(1):51–57. doi: 10.3168/jds.s0022-0302(72)85431-6. [DOI] [PubMed] [Google Scholar]
  67. Keenan T. W., Morré D. J., Cheetham R. D. Lactose synthesis by a golgi apparatus fraction from rat mammary gland. Nature. 1970 Dec 12;228(5276):1105–1106. doi: 10.1038/2281105a0. [DOI] [PubMed] [Google Scholar]
  68. Keenan T. W., Morré D. J., Olson D. E., Yunghans W. N., Patton S. Biochemical and morphological comparison of plasma membrane and milk fat globule membrane from bovine mammary gland. J Cell Biol. 1970 Jan;44(1):80–93. doi: 10.1083/jcb.44.1.80. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Kennel S. J., Lerner R. A. Isolation and characterization of plasma membrane associated immunoglobulin from cultured human diploid lymphocytes. J Mol Biol. 1973 Jun 5;76(4):485–502. doi: 10.1016/0022-2836(73)90487-7. [DOI] [PubMed] [Google Scholar]
  70. Kornguth S. E., Sunderland E. Isolation and partial characterization of a tubulin-like protein from human and swine synaptosomal membranes. Biochim Biophys Acta. 1975 May 30;393(1):100–114. doi: 10.1016/0005-2795(75)90220-2. [DOI] [PubMed] [Google Scholar]
  71. Kuhn C., 3rd, Callaway L. A., Askin F. B. The formation of granules in the bronchiolar Clara cells of the rat. 1. Electron microscopy,. J Ultrastruct Res. 1974 Dec;49(3):387–400. doi: 10.1016/s0022-5320(74)90052-5. [DOI] [PubMed] [Google Scholar]
  72. Kurosumi K., Kobayashi Y., Baba N. The fine structure of mammary glands of lactating rats, with special reference to the apocrine secretion. Exp Cell Res. 1968 Apr;50(1):177–192. doi: 10.1016/0014-4827(68)90406-0. [DOI] [PubMed] [Google Scholar]
  73. LUFT J. H. Improvements in epoxy resin embedding methods. J Biophys Biochem Cytol. 1961 Feb;9:409–414. doi: 10.1083/jcb.9.2.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Lagunoff D., Curran D. E. Role of bristle-coated membrane in the uptake of ferritin by rat macrophages. Exp Cell Res. 1972 Dec;75(2):337–346. doi: 10.1016/0014-4827(72)90438-7. [DOI] [PubMed] [Google Scholar]
  75. Lazarides E., Weber K. Actin antibody: the specific visualization of actin filaments in non-muscle cells. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2268–2272. doi: 10.1073/pnas.71.6.2268. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Le Marchand Y., Singh A., Assimacopoulos-Jeannet F., Orci L., Rouiller C., Jeanrenaud B. A role for the microtubular system in the release of very low density lipoproteins by perfused mouse livers. J Biol Chem. 1973 Oct 10;248(19):6862–6870. [PubMed] [Google Scholar]
  77. Lenard J., Compans R. W. The membrane structure of lipid-containing viruses. Biochim Biophys Acta. 1974 Apr 8;344(1):51–94. doi: 10.1016/0304-4157(74)90008-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Linzell J. L., Peaker M. Intracellular concentrations of sodium, potassium and chloride in the lactating mammary gland and their relation to the secretory mechanism. J Physiol. 1971 Aug;216(3):683–700. doi: 10.1113/jphysiol.1971.sp009547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Linzell J. L., Peaker M. Mechanism of milk secretion. Physiol Rev. 1971 Jul;51(3):564–597. doi: 10.1152/physrev.1971.51.3.564. [DOI] [PubMed] [Google Scholar]
  80. Linzell J. L., Peaker M. The permeability of mammary ducts. J Physiol. 1971 Aug;216(3):701–716. doi: 10.1113/jphysiol.1971.sp009548. [DOI] [PMC free article] [PubMed] [Google Scholar]
  81. Mabuchi I. A myosin-like protein in the cortical layer of the sea urchin egg. J Cell Biol. 1973 Nov;59(2 Pt 1):542–547. doi: 10.1083/jcb.59.2.542. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Mather I. H., Keenan T. W. Studies on the structure of milk fat globule membrane. J Membr Biol. 1975 Apr 23;21(1-2):65–85. doi: 10.1007/BF01941062. [DOI] [PubMed] [Google Scholar]
  83. Meldolesi J. Secretory mechanisms in pancreatic acinar cells. Role of the cytoplasmic membranes. Adv Cytopharmacol. 1974;2:71–85. [PubMed] [Google Scholar]
  84. Morré D. J., Keenan T. W., Huang C. M. Membrane flow and differentiation: origin of Golgi apparatus membranes from endoplasmic reticulum. Adv Cytopharmacol. 1974;2:107–125. [PubMed] [Google Scholar]
  85. Mukherjee T. M., Staehelin L. A. The fine-structural organization of the brush border of intestinal epithelial cells. J Cell Sci. 1971 May;8(3):573–599. doi: 10.1242/jcs.8.3.573. [DOI] [PubMed] [Google Scholar]
  86. Murray R. L., Dubin M. W. The occurrence of actinlike filaments in association with migrating pigment granules in frog retinal pigment epithelium. J Cell Biol. 1975 Mar;64(3):705–710. doi: 10.1083/jcb.64.3.705. [DOI] [PMC free article] [PubMed] [Google Scholar]
  87. Nagasawa J., Douglas W. W., Schulz R. A. Micropinocytotic origin of coated and smooth microvesicles ("synaptic vesicles") in neurosecretory terminals of posterior pituitary glands demonstrated by incorporation of horseradish peroxidase. Nature. 1971 Jul 30;232(5309):341–342. doi: 10.1038/232341a0. [DOI] [PubMed] [Google Scholar]
  88. Nève P., Willems C., Dumont J. E. Involvement of the microtubule-microfilament system in thyroid secretion. Exp Cell Res. 1970 Dec;63(2):457–460. doi: 10.1016/0014-4827(70)90238-7. [DOI] [PubMed] [Google Scholar]
  89. Olsen B. R., Prockop D. J. Ferritin-conjugated antibodies used for labeling of organelles involved in the cellular synthesis and transport of procollagen. Proc Natl Acad Sci U S A. 1974 May;71(5):2033–2037. doi: 10.1073/pnas.71.5.2033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. Orci L., Like A. A., Amherdt M., Blondel B., Kanazawa Y., Marliss E. B., Lambert A. E., Wollheim C. B., Renold A. E. Monolayer cell culture of neonatal rat pancreas: an ultrastructural and biochemical study of functioning endocrine cells. J Ultrastruct Res. 1973 May;43(3):270–297. doi: 10.1016/s0022-5320(73)80039-5. [DOI] [PubMed] [Google Scholar]
  91. Palade G. E., Bruns R. R. Structural modulations of plasmalemmal vesicles. J Cell Biol. 1968 Jun;37(3):633–649. doi: 10.1083/jcb.37.3.633. [DOI] [PMC free article] [PubMed] [Google Scholar]
  92. Patton S., Fowkes F. M. The role of the plasma membrane in the secretion of milk fat. J Theor Biol. 1967 Jun;15(3):274–281. doi: 10.1016/0022-5193(67)90137-3. [DOI] [PubMed] [Google Scholar]
  93. Patton S. Reversible suppression of lactation by colchicine. FEBS Lett. 1974 Nov 1;48(1):85–87. doi: 10.1016/0014-5793(74)81068-9. [DOI] [PubMed] [Google Scholar]
  94. Pitelka D. R., Hamamoto S. T., Duafala J. G., Nemanic M. K. Cell contacts in the mouse mammary gland. I. Normal gland in postnatal development and the secretory cycle. J Cell Biol. 1973 Mar;56(3):797–818. doi: 10.1083/jcb.56.3.797. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Pitelka D. R., Kerkof P. R., Gagné H. T., Smith S., Abraham S. Characteristics of cells dissociated from mouse mammary glands. I. Method of separation and morphology of parenchymal cells from lactating glands. Exp Cell Res. 1969 Sep;57(1):43–62. doi: 10.1016/0014-4827(69)90365-6. [DOI] [PubMed] [Google Scholar]
  96. Pollard T. D., Ito S. Cytoplasmic filaments of Amoeba proteus. I. The role of filaments in consistency changes and movement. J Cell Biol. 1970 Aug;46(2):267–289. doi: 10.1083/jcb.46.2.267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  97. REYNOLDS E. S. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol. 1963 Apr;17:208–212. doi: 10.1083/jcb.17.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  98. RICHARDSON K. C. Contractile tissues in the mammary gland, with special reference to myoepithelium in the goat. Proc R Soc Lond B Biol Sci. 1949 May 9;136(882):30–45. doi: 10.1098/rspb.1949.0004. [DOI] [PubMed] [Google Scholar]
  99. ROTH T. F., PORTER K. R. YOLK PROTEIN UPTAKE IN THE OOCYTE OF THE MOSQUITO AEDES AEGYPTI. L. J Cell Biol. 1964 Feb;20:313–332. doi: 10.1083/jcb.20.2.313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  100. Reaven E. P., Axline S. G. Subplasmalemmal microfilaments and microtubules in resting and phagocytizing cultivated macrophages. J Cell Biol. 1973 Oct;59(1):12–27. doi: 10.1083/jcb.59.1.12. [DOI] [PMC free article] [PubMed] [Google Scholar]
  101. Redman C. M., Banerjee D., Howell K., Palade G. E. Colchicine inhibition of plasma protein release from rat hepatocytes. J Cell Biol. 1975 Jul;66(1):42–59. doi: 10.1083/jcb.66.1.42. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Riordan J. R., Mitranic M., Slavik M., Moscarello M. A. The incorporation of L-(14C) fucose into glycoprotein fractions of liver plasma membranes. FEBS Lett. 1974 Oct 15;47(2):248–251. doi: 10.1016/0014-5793(74)81022-7. [DOI] [PubMed] [Google Scholar]
  103. Robison W. G., Jr, Charlton J. S. Microtubules, microfilaments, and pigment movement in the chromatophores of Palaemonetes vulgaris (Crustacea). J Exp Zool. 1973 Dec;186(3):279–304. doi: 10.1002/jez.1401860307. [DOI] [PubMed] [Google Scholar]
  104. Rohrlich S. T. Fine structural demonstration of ordered arrays of cytoplasmic filaments in vertebrate iridophores. A comparative survey. J Cell Biol. 1974 Aug;62(2):295–304. doi: 10.1083/jcb.62.2.295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  105. Roth L. E., Pihlaja D. J., Shigenaka Y. Microtubules in the heliozoan axopodium. I. The gradion hypothesis of allosterism in structural proteins. J Ultrastruct Res. 1970 Jan;30(1):7–37. doi: 10.1016/s0022-5320(70)90062-6. [DOI] [PubMed] [Google Scholar]
  106. SLAUTTERBACK D. B. CYTOPLASMIC MICROTUBULES. I. HYDRA. J Cell Biol. 1963 Aug;18:367–388. doi: 10.1083/jcb.18.2.367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. Satir B. Membrane events during the secretory process. Symp Soc Exp Biol. 1974;(28):399–418. [PubMed] [Google Scholar]
  108. Satir B., Schooley C., Satir P. Membrane fusion in a model system. Mucocyst secretion in Tetrahymena. J Cell Biol. 1973 Jan;56(1):153–176. doi: 10.1083/jcb.56.1.153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Schmidt D. G., Both P., van Markwijk B. W., Buchheim W. The determination of size and molecular weight of casein micelles by means of light-scattering and electron microscopy. Biochim Biophys Acta. 1974 Sep 13;365(1):72–79. doi: 10.1016/0005-2795(74)90251-7. [DOI] [PubMed] [Google Scholar]
  110. Sekhri K. K., Pitelka D. R., DeOme K. B. Studies of mouse mammary glands. I. Cytomorphology of the normal mammary gland. J Natl Cancer Inst. 1967 Sep;39(3):459–490. [PubMed] [Google Scholar]
  111. Selman G. G., Perry M. M. Ultrastructural changes in the surface layers of the newt's egg in relation to the mechanism of its cleavage. J Cell Sci. 1970 Jan;6(1):207–227. doi: 10.1242/jcs.6.1.207. [DOI] [PubMed] [Google Scholar]
  112. Silcock W. R., Patton S. Correlative secretion of protein, lactose and K + in milk of the goat. J Cell Physiol. 1972 Feb;79(1):151–154. doi: 10.1002/jcp.1040790118. [DOI] [PubMed] [Google Scholar]
  113. Slautterback D. B. Coated vesicles in absorptive cells of Hydra. J Cell Sci. 1967 Dec;2(4):563–572. doi: 10.1242/jcs.2.4.563. [DOI] [PubMed] [Google Scholar]
  114. Smith D. S. On the significance of cross-bridges between microtubules and synaptic vesicles. Philos Trans R Soc Lond B Biol Sci. 1971 Jun 17;261(839):395–405. doi: 10.1098/rstb.1971.0074. [DOI] [PubMed] [Google Scholar]
  115. Stadler J., Franke W. W. Characterization of the colchicine binding of membrane fractions from rat and mouse liver. J Cell Biol. 1974 Jan;60(1):297–303. doi: 10.1083/jcb.60.1.297. [DOI] [PMC free article] [PubMed] [Google Scholar]
  116. Stein O., Stein Y. Colchicine-induced inhibition of very low density lipoprotein release by rat liver in vivo. Biochim Biophys Acta. 1973 Apr 13;306(1):142–147. doi: 10.1016/0005-2760(73)90219-1. [DOI] [PubMed] [Google Scholar]
  117. Stewart P. S., Puppione D. L., Patton S. The presence of microvilli and other membrane fragments in the non-fat phase of bovine milk. Z Zellforsch Mikrosk Anat. 1972;123(2):161–167. doi: 10.1007/BF02583470. [DOI] [PubMed] [Google Scholar]
  118. Trump B. F., Bulger R. E. New ultrastructural characteristics of cells fixed in a glutaraldehyde-osmium tetroxide mixture. Lab Invest. 1966 Jan;15(1 Pt 2):368–379. [PubMed] [Google Scholar]
  119. VENABLE J. H., COGGESHALL R. A SIMPLIFIED LEAD CITRATE STAIN FOR USE IN ELECTRON MICROSCOPY. J Cell Biol. 1965 May;25:407–408. doi: 10.1083/jcb.25.2.407. [DOI] [PMC free article] [PubMed] [Google Scholar]
  120. Vitetta E. S., Uhr J. W. Immunoglobulins and alloantigens on the surface of lymphoid cells. Biochim Biophys Acta. 1975 Jun 30;415(2):253–271. doi: 10.1016/0304-4157(75)90004-0. [DOI] [PubMed] [Google Scholar]
  121. WELLINGS S. R., DEOME K. B. Milk protein droplet formation in the Golgi apparatus of the C3H/Crgl mouse mammary epithelial cells. J Biophys Biochem Cytol. 1961 Feb;9:479–485. doi: 10.1083/jcb.9.2.479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  122. WELLINGS S. R., DEOME K. B., PITELKA D. R. Electron microscopy of milk secretion in the mammary gland of the C3H/Crgl mouse. I. Cytomorphology of the prelactating and the lactating gland. J Natl Cancer Inst. 1960 Aug;25:393–421. [PubMed] [Google Scholar]
  123. WELLINGS S. R., PHILP J. R. THE FUNCTION OF THE GOLGI APPARATUS IN LACTATING CELLS OF THE BALB/CCRGL MOUSE. AN ELECTRON MICROSCOPIC AND AUTORADIOGRAPHIC STUDY. Z Zellforsch Mikrosk Anat. 1964 Jan 31;61:871–882. doi: 10.1007/BF00340040. [DOI] [PubMed] [Google Scholar]
  124. Wallach D., Kirshner N., Schramm M. Non-parallel transport of membrane proteins and content proteins during assembly of the secretory granule in rat parotid gland. Biochim Biophys Acta. 1975 Jan 14;375(1):87–105. doi: 10.1016/0005-2736(75)90074-7. [DOI] [PubMed] [Google Scholar]
  125. Wooding F. B. Formation of the milk fat globule membrane without participation of the plasmalemma. J Cell Sci. 1973 Jul;13(1):221–235. doi: 10.1242/jcs.13.1.221. [DOI] [PubMed] [Google Scholar]
  126. Wooding F. B. The mechanism of secretion of the milk fat globule. J Cell Sci. 1971 Nov;9(3):805–821. doi: 10.1242/jcs.9.3.805. [DOI] [PubMed] [Google Scholar]
  127. Wooding F. B. The structure of the milk fat globule membrane. J Ultrastruct Res. 1971 Nov;37(3):388–400. doi: 10.1016/s0022-5320(71)80133-8. [DOI] [PubMed] [Google Scholar]

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