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PMID: 12952080 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

AmpA, a modular protein containing disintegrin and ornatin domains, has multiple effects on cell adhesion and cell fate specification.

Journal of muscle research and cell motility ·Vol. 23 ·No. 7-8 ·2002-00-00 ·Pages 817-28

Blumberg DD, Ho HN, Petty CL, Varney TR, Gandham S

Abstract

Proteins containing disintegrin domains play a variety of roles in regulating processes involving adhesion, migration and cell type specification during development of many metazoan organisms. Most disintegrin domain containing proteins belong to the ADAM (a disintegrin and a metalloprotease) family of proteins that also contain a metalloprotease domain. Here we describe a small secreted protein from Dictyostelium that contains multiple repeated domains sharing homology with both the disintegrin motif and with a second class of fibrinogen receptor antagonists, the ornatins. This protein, called AmpA for its role in modulating adhesion, differs from the ADAM family proteins in that it lacks a metalloprotease domain. Nonetheless, it appears to be involved in the same complex spectrum of developmental functions as the metazoan ADAM family proteins. Here we review the structure and evolution of this protein and its function in cell adhesion and cell type specification. We discuss possible mechanisms by which it might function and review the emerging evidence for a close coupling between cell adhesion and cell type specification.

MeSH Terms
Amino Acid Sequence Animals Cell Adhesion/physiology Dictyostelium/cytology,physiology Disintegrins/chemistry,metabolism Invertebrate Hormones/metabolism Mammals Metalloendopeptidases/metabolism Molecular Sequence Data Movement/physiology Protozoan Proteins/chemistry,metabolism Sequence Alignment Sequence Homology, Amino Acid
Chemicals
Disintegrins Invertebrate Hormones Protozoan Proteins ornatin AmpA protein, Dictyostelium protozoan Metalloendopeptidases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Blumberg Daphne D
Department of Biological Sciences, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, USA. [email protected]
Ho Hoa N
Petty Chere' L
Varney Timothy R
Gandham Srilatha
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Article Info
Journal
Journal of muscle research and cell motility
Abbr.
J Muscle Res Cell Motil
ISSN
0142-4319
Published
2002-00-00
Pages
817-28
Language
English
Region
Netherlands
NLM ID
8006298
Subset
IM
Grants
NIGMS NIH HHS · R01GM56690 · United States
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