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Gene Review

A2M  -  alpha-2-macroglobulin

Bos taurus

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Disease relevance of A2M


High impact information on A2M

  • Double-label experiments using beta-galactosidase and gold/alpha 2-macroglobulin showed the presence of the two ligands in the same coated pits and receptosomes [2].
  • Thus, the pathway for internalization of beta-galactosidase via the mannose 6-phosphate receptor is similar to the pathway established for other ligands such as low density lipoprotein and alpha 2-macroglobulin [2].
  • The addition of alpha 2-macroglobulin to serum-free medium or to antiprotease-depleted serum resulted in the blockage of morphological responses of Sertoli cells to FSH or to dbcAMP [3].
  • Addition of alpha 2-macroglobulin blocked the inhibitory effects of dbcAMP on Sertoli cell migration [3].
  • The conformational changes around the thioester-bond region of human or bovine alpha 2M (alpha 2-macroglobulin) on reaction with methylamine or trypsin were studied with the probe AEDANS [N-(acetylaminoethyl)-8-naphthylamine-1-sulphonic acid], bound to the liberated thiol groups [4].

Biological context of A2M


Anatomical context of A2M


Associations of A2M with chemical compounds


Physical interactions of A2M


Other interactions of A2M


Analytical, diagnostic and therapeutic context of A2M

  • Gel filtration experiments demonstrated that in Pedersen fetuin PDGF occurred both free, and in association with alpha 2-macroglobulin [5].
  • Conformational alterations occurring in bovine alpha 2-macroglobulin (alpha 2M) resulting from proteolysis and nucleophilic modification have been monitored by UV difference spectra, circular dichroism, and changes in the fluorescence of 6-(p-toluidino)-2-naphthalenesulfonate (TNS) and bis(8-anilino-1-naphthalenesulfonate) (Bis-ANS) [19].
  • Sequence analysis of several internal peptides confirms that the tick protein belongs to the alpha-2-macroglobulin family, and the protein is therefore referred to as tick alpha-macroglobulin (TAM) [7].
  • We cloned and sequenced a PCR product containing sequences from both subunits and spanning the N-terminus of subunit B and the putative 'bait region' (a segment of alpha-2-macroglobulin which serves as target for various proteases) [7].
  • The immunoassay was affected both by alkaline denaturation, which is a common feature of aspartic proteinases, and by the presence of the proteinase scavenger alpha-2-macroglobulin [20].


  1. Isolation and characterization of alpha 2-macroglobulin from mastitis milk. Rantamäki, L.K., Müller, H.P. J. Dairy Res. (1992) [Pubmed]
  2. Morphologic study of the internalization of a lysosomal enzyme by the mannose 6-phosphate receptor in cultured Chinese hamster ovary cells. Willingham, M.C., Pastan, I.H., Sahagian, G.G., Jourdian, G.W., Neufeld, E.F. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  3. Proteases are implicated in the changes in the Sertoli cell cytoskeleton elicited by follicle-stimulating hormone or by dibutyryl cyclic AMP. Tung, P.S., Burdzy, K., Fritz, I.B. J. Cell. Physiol. (1993) [Pubmed]
  4. The conformational changes of alpha 2-macroglobulin induced by methylamine or trypsin. Characterization by extrinsic and intrinsic spectroscopic probes. Larsson, L.J., Lindahl, P., Hallén-Sandgren, C., Björk, I. Biochem. J. (1987) [Pubmed]
  5. Analysis of the mitogenic effect of fetuin preparations on arterial smooth muscle cells: the role of contaminant platelet-derived growth factor. Libby, P., Raines, E.W., Cullinane, P.M., Ross, R. J. Cell. Physiol. (1985) [Pubmed]
  6. Receptor-mediated endocytosis of alpha 2-macroglobulin and transferrin in rat caput epididymal epithelial cells in vitro. Djakiew, D., Byers, S.W., Dym, M. Biol. Reprod. (1984) [Pubmed]
  7. Characterization of an alpha-macroglobulin-like glycoprotein isolated from the plasma of the soft tick Ornithodoros moubata. Kopácek, P., Weise, C., Saravanan, T., Vítová, K., Grubhoffer, L. Eur. J. Biochem. (2000) [Pubmed]
  8. Time-course levels of alpha 2-macroglobulin and albumin in cow colostrum and milk and alpha 2-macroglobulin levels in mastitic cow milk. Perez, M.D., Sanchez, L., Aranda, P., Sala, F.J., Calvo, M. Ann. Rech. Vet. (1989) [Pubmed]
  9. In vitro modulation of the eosinophil-dependent enhancement of the permeability of the bronchial mucosa. Herbert, C.A., Edwards, D., Boot, J.R., Robinson, C. Br. J. Pharmacol. (1991) [Pubmed]
  10. Sequential limited proteolysis of myelin basic protein by neutral protease activities of bovine brain. Berlet, H.H., Ilzenhöfer, H. J. Neurochem. (1985) [Pubmed]
  11. The structure around the thioester bond in bovine alpha 2-macroglobulin. Possible implications for the conformational stability of the inhibitor on thioester cleavage. Björk, I., Jörnvall, H. FEBS Lett. (1986) [Pubmed]
  12. Variations in the size and sulfation of heparin modulate the effect of heparin on the binding of VEGF165 to its receptors. Soker, S., Goldstaub, D., Svahn, C.M., Vlodavsky, I., Levi, B.Z., Neufeld, G. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  13. Inhibition of adrenocortical steroidogenesis by alpha 2-macroglobulin is caused by associated transforming growth factor beta. Keramidas, M., Chambaz, E.M., Feige, J.J. Mol. Cell. Endocrinol. (1992) [Pubmed]
  14. Endothelial cells and components of the kallikrein-kinin system. Ryan, U.S., Ryan, J.W., Habliston, D.L., Pena, G.A. Adv. Exp. Med. Biol. (1979) [Pubmed]
  15. Transforming growth factor beta 1: an autocrine regulator of adrenocortical steroidogenesis. Feige, J.J., Cochet, C., Savona, C., Shi, D.L., Keramidas, M., Defaye, G., Chambaz, E.M. Endocr. Res. (1991) [Pubmed]
  16. Role of complement S protein (vitronectin) in adherence of Streptococcus dysgalactiae to bovine epithelial cells. Filippsen, L.F., Valentin-Weigand, P., Blobel, H., Preissner, K.T., Chhatwal, G.S. Am. J. Vet. Res. (1990) [Pubmed]
  17. Hemostatic profile of bovine ovarian follicular fluid. Yamada, M., Gentry, P.A. Can. J. Physiol. Pharmacol. (1995) [Pubmed]
  18. Cleavage of proteins of reproductive secretions by extracellular proteinases of Tritrichomonas foetus. Talbot, J.A., Nielsen, K., Corbeil, L.B. Can. J. Microbiol. (1991) [Pubmed]
  19. Fluorescent probes as a measure of conformational alterations induced by nucleophilic modification and proteolysis of bovine alpha 2-macroglobulin. Strickland, D.K., Steiner, J.P., Feldman, S.R., Pizzo, S.V. Biochemistry (1984) [Pubmed]
  20. Detection of Candida proteinase by enzyme immunoassay and interaction of the enzyme with alpha-2-macroglobulin. Rüchel, R., Böning, B. J. Immunol. Methods (1983) [Pubmed]
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