The involvement of the fibronectin type II-like modules of human gelatinase A in cell surface localization and activation.

doi:10.1074/jbc.273.32.20622

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

The involvement of the fibronectin type II-like modules of human gelatinase A in cell surface localization and activation.

The Journal of biological chemistry - 7 Aug 1998

Steffensen B, Bigg H F, Overall C M

Abstract excerpt

Recombinant collagen-binding domain (rCBD) comprising the three fibronectin type II-like modules of human gelatinase A was found to compete the zymogen form of this matrix metalloproteinase from the cell surface of normal human fibroblasts in culture. Upon concanavalin A treatment of cells, the i...

Topics

Antibodies
Binding, Competitive
Cell Adhesion
Collagen
Collagenases
Concanavalin A
Enzyme Activation
Enzyme Precursors
Fibroblasts
Fibronectins
Gelatinases
Gingiva

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Heparin

Humans

Integrin beta1

Matrix Metalloproteinase 2

Metalloendopeptidases

Microscopy, Electron, Scanning

Source

Open in PubMed

Identifiers

PMID: 9685420
DOI: 10.1074/jbc.273.32.20622

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9685420-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The involvement of the fibronectin type II-like modules of human gelatinase A in cell surface localization and activation.PMID 9685420Read ↗

The Fibronectin Extra Domain A Activates Matrix Metalloproteinase Gene Expression by an Interleukin-1-dependent MechanismSemantic proximity Read ↗

Contributions of the MMP-2 collagen binding domain to gelatin cleavage. Substrate binding via the collagen binding domain is required for hydrolysis of gelatin but not short peptides.Semantic proximity Read ↗

Functional basis for the overlap in ligand interactions and substrate specificities of matrix metalloproteinases-9 and -2.Semantic proximity Read ↗

Syndecan-1 supports integrin alpha2beta1-mediated adhesion to collagen.Semantic proximity Read ↗

Growth factor and co-receptor release by structural regulation of substrate metalloprotease accessibility.Semantic proximity Read ↗

C-type lectin-like domain and fibronectin-like type II domain of phospholipase A(2) receptor 1 modulate binding and migratory responses to collagen.Semantic proximity Read ↗

Concanavalin A produces a matrix-degradative phenotype in human fibroblasts. Induction and endogenous activation of collagenase, 72-kDa gelatinase, and Pump-1 is accompanied by the suppression of the tissue inhibitor of matrix metalloproteinases.Semantic proximity Read ↗

The hemopexin domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) Is not required for its activation of proMMP2 on cell surface but is essential for MT1-MMP-mediated invasion in three-dimensional type I collagen.Semantic proximity Read ↗

Regulation of fibroblast migration on collagenous matrix by a cell surface peptidase complex.Semantic proximity Read ↗

Two synergistic activation mechanisms of alpha2beta1 integrin-mediated collagen binding.Semantic proximity Read ↗

Trench-shaped Binding Sites Promote Multiple Classes of Interactions between Collagen and the Adherence Receptors, α1β1 Integrin and Staphylococcus aureus Cna MSCRAMMSemantic proximity Read ↗

Cell surface adhesion of pregnancy‐associated plasma protein‐A is mediated by four clusters of basic residues located in its third and fourth CCP moduleSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.