Skip to main content
NCBI home page
British Journal of Experimental Pathology logoLink to British Journal of Experimental Pathology
. 1988 Oct;69(5):605–619.

Biochemical nature and cellular origin of amyloid enhancing factor (AEF) as determined by anti-AEF antibody.

K Alizadeh-Khiavi 1, Z Ali-Khan 1
PMCID: PMC2013270  PMID: 3058197

Abstract

Low ionic strength acidic buffer, Sephadex G-200 and Benzamidine-Sepharose (BZ) gel chromatography, have been used for the partial purification of alveolar hydatid cyst (AHC) induced amyloid enhancing factor (AEF). BZ-gel bound AEF (AEF-BZ) demonstrated AEF activity in the mouse bioassay, proteolytic activity against Hide powder azure showed two major and three minor peptides on SDS-PAGE. Pretreatment of AEF-BZ with 10 mM phenylmethylsulphonyl fluoride or 20 mM p-chloromercuribenzoic acid completely abolished its bioactivity in vivo and proteolytic activity in vitro. Polyclonal anti-AEF antibody (AAA) was generated which on passive transfer into mice completely abolished the bioactivity of both casein-induced, or AHC-induced AEF. The AAA absorbed on Sepharose gel conjugated to normal mouse serum developed one common precipitin band between AE and AEF-positive sera from AHC-infected and old retired mice and in immunostaining it bound to the cytoplasmic granular components of a majority of splenic and peritoneal leucocytes from AHC-infected mice. In contrast, only a few normal mouse leucocytes showed positive staining. We suggest that AEF, in all probability, is a serine/thiol protease of leucocyte origin whose intracellular and humoral concentrations increase significantly during amyloidosis. The role of lysosomal proteases and anti-AEF antibody which has been successfully generated for the first time is discussed with reference to the origin of AEF and its presumed biological function in amyloidogenesis.

Full text

PDF
605

Images in this article

611Fig. 2
on p.611
612Fig. 3
on p.612
613Fig. 4
on p.613

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ali-Khan Z. Cellular changes in the lymphoreticular tissues of C57L/J mice infected with Echinococcus multilocularis cysts. Immunology. 1978 May;34(5):831–839. [PMC free article] [PubMed] [Google Scholar]
  2. Ali-Khan Z., Jothy S., Al-Karmi T. Murine alveolar hydatidosis: a potential experimental model for the study of AA-amyloidosis. Br J Exp Pathol. 1983 Dec;64(6):599–611. [PMC free article] [PubMed] [Google Scholar]
  3. Ali-Khan Z., Siboo R. Immune complexes in experimental alveolar hydatidosis. Tropenmed Parasitol. 1983 Sep;34(3):187–192. [PubMed] [Google Scholar]
  4. Ali-Khan Z., Siboo R. Pathogenesis and host response in subcutaneous alveolar hydatidosis. I. Histogenesis of alveolar cyst and a qualitative analysis of the inflammatory infiltrates. Z Parasitenkd. 1980;62(3):241–254. doi: 10.1007/BF00926565. [DOI] [PubMed] [Google Scholar]
  5. Alkarmi T. O., Ali-Khan Z. Chronic alveolar hydatidosis and secondary amyloidosis: pathological aspects of the disease in four strains of mice. Br J Exp Pathol. 1984 Aug;65(4):405–417. [PMC free article] [PubMed] [Google Scholar]
  6. Axelrad M. A., Kisilevsky R., Willmer J., Chen S. J., Skinner M. Further characterization of amyloid-enhancing factor. Lab Invest. 1982 Aug;47(2):139–146. [PubMed] [Google Scholar]
  7. Eriksen N., Ericsson L. H., Pearsall N., Lagunoff D., Benditt E. P. Mouse amyloid protein AA: Homology with nonimmunoglobulin protein of human and monkey amyloid substance. Proc Natl Acad Sci U S A. 1976 Mar;73(3):964–967. doi: 10.1073/pnas.73.3.964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fritz H., Jochum M., Geiger R., Duswald K. H., Dittmer H., Kortmann H., Neumann S., Lang H. Granulocyte proteinases as mediators of unspecific proteolysis in inflammation: a review. Folia Histochem Cytobiol. 1986;24(2):99–115. [PubMed] [Google Scholar]
  9. Fuks A., Zucker-Franklin D. Impaired Kupffer cell function precedes development of secondary amyloidosis. J Exp Med. 1985 May 1;161(5):1013–1028. doi: 10.1084/jem.161.5.1013. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. GOLD A. M. SULFONYL FLUORIDES AS INHIBITORS OF ESTERASES. 3. IDENTIFICATION OF SERINE AS THE SITE OF SULFONYLATION IN PHENYLMETHANESULFONYL ALPHA-CHYMOTRYPSIN. Biochemistry. 1965 May;4:897–901. doi: 10.1021/bi00881a016. [DOI] [PubMed] [Google Scholar]
  11. Hardt F., Ranlov P. Transfer amyloidosis. Int Rev Exp Pathol. 1976;16:273–334. [PubMed] [Google Scholar]
  12. Hol P. R., van Ederen A. M., Snel F. W., Langeveld J. P., Veerkamp J. H., Gruys E. Activities of lysosomal enzymes and levels of serum amyloid A (SAA) in blood plasma of hamsters during casein induction of AA-amyloidosis. Br J Exp Pathol. 1985 Jun;66(3):279–292. [PMC free article] [PubMed] [Google Scholar]
  13. James G. T. Inactivation of the protease inhibitor phenylmethylsulfonyl fluoride in buffers. Anal Biochem. 1978 Jun 1;86(2):574–579. doi: 10.1016/0003-2697(78)90784-4. [DOI] [PubMed] [Google Scholar]
  14. Janigan D. T., Druet R. L. Experimental murine amyloidosis in x-irradiated recipients of spleen homogenates or serum from sensitized donors. Am J Pathol. 1968 Feb;52(2):381–390. [PMC free article] [PubMed] [Google Scholar]
  15. Kazimierczak J. Cytochemical study of casein-induced and nitrogen mustard accelerated amyloidosis in mice. Acta Pathol Microbiol Scand. 1969;77(2):201–217. doi: 10.1111/j.1699-0463.1969.tb04225.x. [DOI] [PubMed] [Google Scholar]
  16. Kisilevsky R., Axelrad M., Corbett W., Brunet S., Scott F. The role of inflammatory cells in the pathogenesis of amyloidosis. Lab Invest. 1977 Dec;37(6):544–553. [PubMed] [Google Scholar]
  17. Kisilevsky R., Boudreau L., Foster D. Kinetics of amyloid deposition. II. The effects of dimethylsulfoxide and colchicine therapy. Lab Invest. 1983 Jan;48(1):60–67. [PubMed] [Google Scholar]
  18. Lavie G., Zucker-Franklin D., Franklin E. C. Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes. J Exp Med. 1978 Oct 1;148(4):1020–1031. doi: 10.1084/jem.148.4.1020. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Levin M., Franklin E. C., Frangione B., Pras M. The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest. 1972 Oct;51(10):2773–2776. doi: 10.1172/JCI107098. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Li C. Y., Lam K. W., Yam L. T. Esterases in human leukocytes. J Histochem Cytochem. 1973 Jan;21(1):1–12. doi: 10.1177/21.1.1. [DOI] [PubMed] [Google Scholar]
  21. Ragsdale C. G., Arend W. P. Neutral protease secretion by human monocytes. Effect of surface-bound immune complexes. J Exp Med. 1979 Apr 1;149(4):954–968. doi: 10.1084/jem.149.4.954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Rinderknecht H., Geokas M. C., Silverman P., Haverback B. J. A new ultrasensitive method for the determination of proteolytic activity. Clin Chim Acta. 1968 Aug;21(2):197–203. doi: 10.1016/0009-8981(68)90127-7. [DOI] [PubMed] [Google Scholar]
  23. Schnyder J., Baggiolini M. Secretion of lysosomal hydrolases by stimulated and nonstimulated macrophages. J Exp Med. 1978 Aug 1;148(2):435–450. doi: 10.1084/jem.148.2.435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Silverman S. L., Cathcart E. S., Skinner M., Cohen A. S. The degradation of serum amyloid A protein by activated polymorphonuclear leucocytes: participation of granulocytic elastase. Immunology. 1982 Aug;46(4):737–744. [PMC free article] [PubMed] [Google Scholar]
  25. Sipe J. D., McAdam K. P., Uchino F. Biochemical evidence for the biphasic development of experimental amyloidosis. Lab Invest. 1978 Jan;38(1):110–114. [PubMed] [Google Scholar]
  26. Skogen B., Natvig J. B. Degradation of amyloid proteins by different serine proteases. Scand J Immunol. 1981 Oct;14(4):389–396. doi: 10.1111/j.1365-3083.1981.tb00579.x. [DOI] [PubMed] [Google Scholar]
  27. Werb Z., Chin J. R. Apoprotein E is synthesized and secreted by resident and thioglycollate-elicited macrophages but not by pyran copolymer- or bacillus Calmette-Guerin-activated macrophages. J Exp Med. 1983 Oct 1;158(4):1272–1293. doi: 10.1084/jem.158.4.1272. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Werb Z. How the macrophage regulates its extracellular environment. Am J Anat. 1983 Mar;166(3):237–256. doi: 10.1002/aja.1001660302. [DOI] [PubMed] [Google Scholar]

Articles from British journal of experimental pathology are provided here courtesy of Wiley

RESOURCES