Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide

Gregory A. Bannikov, Tatiana V. Karelina, Ivan E. Collier, Barry L. Marmer, Gregory I. Goldberg

Research output: Contribution to journalArticlepeer-review

122 Scopus citations


Expression of gelatinase B (matrix metalloprotease 9) in human placenta is developmentally regulated, presumably to fulfill a proteolytic function. Here we demonstrate that gelatinolytic activity in situ, in tissue sections of term placenta, is co-localized with gelatinase B. Judging by molecular mass, however, all the enzyme extracted from this tissue was found in a proform. To address this apparent incongruity, we examined the activity of gelatinase B bound to either gelatin- or type IV collagen-coated surfaces. Surprisingly, we found that upon binding, the purified proenzyme acquired activity against both the fluorogenic peptide (7-methoxycoumarin-4-yl)-acetic acid (MCA)-Pro-Leu-Gly-Leu-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala- Arg-NH2 and gelatin substrates, whereas its propeptide remained intact. These results suggest that although activation of all known matrix metalloproteases in vitro is accomplished by proteolytic processing of the propeptide, other mechanisms, such as binding to a ligand or to a substrate, may lead to a disengagement of the propeptide from the active center of the enzyme, causing its activation.

Original languageEnglish
Pages (from-to)16022-16027
Number of pages6
JournalJournal of Biological Chemistry
Issue number18
StatePublished - May 3 2002


Dive into the research topics of 'Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide'. Together they form a unique fingerprint.

Cite this