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Alpha-macroglobulins: structure, shape, and mechanism of proteinase complex formation.

Lars Sottrup-Jensen
- 15 Jul 1989 - 
- Vol. 264, Iss: 20, pp 11539-11542
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This article is published in Journal of Biological Chemistry.The article was published on 1989-07-15 and is currently open access. It has received 665 citations till now. The article focuses on the topics: Macroglobulins.

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Matrix Metalloproteinases: A Review

TL;DR: The present review discusses in detail the primary structures and the overlapping yet distinct substrate specificities of MMPs as well as the mode of activation of the unique MMP precursors.
Journal ArticleDOI

Regulation of matrix metalloproteinases: an overview.

TL;DR: The recent view about the role of stromal cells in the progression of cancer cell growth and metastasis is particularly interesting, and additional studies about the regulation of MMP gene expression and activity in malignancies are needed to understand the role and regulation ofMMPs in tumor cell invasion.
Journal ArticleDOI

Natural protein proteinase inhibitors and their interaction with proteinases

TL;DR: The structure of pro-carboxypeptidase shows a model of inactivation which bears resemblance to proteinase/protein inhibitor systems, andconsiderable progress in understanding the transition between native and cleaved states of the serpins has also been made by several recent structural studies.
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Serum prostate specific antigen complexed to alpha 1-antichymotrypsin as an indicator of prostate cancer.

TL;DR: The combination of assays measuring total PSA immunoreactivity, the noncomplexed molecular form and PSA in complex with alpha 1-antichymotrypsin may facilitate discrimination between prostate cancer and BPH.
References
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Journal ArticleDOI

Human plasma proteinase inhibitors

TL;DR: This paper presents a meta-analyses of the proton-probes of ATP and its role in the building blocks of proteinase Inhibitor and shows how the role of ATP in the design of proteinases changes with age and disease progression.
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The interaction of α2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism

TL;DR: It is concluded that each molecule of α2-macroglobulin is able to react with one molecule of proteinase only, and there is now reason to believe that α2 -macrogLobulin can bind essentially all proteinases.
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Latent transforming growth factor-beta in serum. A specific complex with alpha 2-macroglobulin.

TL;DR: It is proposed that alpha 2M may serve an important multifunctional role at sites of inflammation by scavenging both active peptides and proteases that are released by platelets at the site of injury.
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STUDIES ON HUMAN PLASMA α2-MACROGLOBULIN-ENZYME INTERACTIONS EVIDENCE FOR PROTEOLYTIC MODIFICATION OF THE SUBUNIT CHAIN STRUCTURE

TL;DR: In this paper, it was found that α2-macroglobulin is comprised of subunit chains of 185,000 molecular weight as analyzed by electrophoresis in polyacrylamide gels containing sodium dodecyl sulfate.
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A thiol-ester in α2-macroglobulin cleaved during proteinase complex formation

TL;DR: The glycoprotein crs-macroglobulin ((YAM), M, 725 000, is unique among plasma proteins in being able to form complexes with proteinases from all 4 classes (EC 3.4 2 1-24) and the function of olM is not well understood.
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