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Gelatinase activity of matrix metalloproteinases in the cerebrospinal fluid of various patient populations.
Res Commun Mol Pathol Pharmacol. 1999; 104(1):42-52.RC

Abstract

We have studied the enzymatic gelatinolytic activity of matrix metalloproteinases (MMPs) present in cerebrospinal fluid (CSF) of samples obtained from 67 individuals, twenty-one nonneurological patients (considered controls) and 46 subjects with various neurological disorders e.g., vascular lesions, demyelination, inflammatory, degenerative and prion diseases. Biochemical characterization of MMPs, a family of neutral proteolytic enzymes involved in extracellular matrix modeling, included determination of substrate specificity and Ca+2 dependency, as well as the effects of protease inactivators, carboxylic and His (histidine) residue modifiers, and antibiotics. Whereas all CSF samples expressed MMP-2 (gelatinase A) activity, it corresponded in most cases (normal and pathological samples) to its latent form (proenzyme; pMMP-2). In general, inflammatory neurological diseases (especially meningitis and neurocisticercosis) were associated with the presence of a second enzyme, MMP-9 (or gelatinase B). Whereas MMP-9 was found in the CSF of every tropical spastic paraparesis patient studied, its presence in samples from individuals with vascular lesions was uncommon. Patients blood-brain barrier damage was ascertained by determining total CSF protein content using both, the conventional polyacrylamide gel electrophoresis procedure under denaturing conditions and capillary zone electrophoresis.

Authors+Show Affiliations

Department of Biochemistry and Molecular Biology, Faculty of Chemical and Pharmaceutical Sciences, University of Chile, Santiago. mavalenz@abello.dic.uchile.clNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10604277

Citation

Valenzuela, M A., et al. "Gelatinase Activity of Matrix Metalloproteinases in the Cerebrospinal Fluid of Various Patient Populations." Research Communications in Molecular Pathology and Pharmacology, vol. 104, no. 1, 1999, pp. 42-52.
Valenzuela MA, Cartier L, Collados L, et al. Gelatinase activity of matrix metalloproteinases in the cerebrospinal fluid of various patient populations. Res Commun Mol Pathol Pharmacol. 1999;104(1):42-52.
Valenzuela, M. A., Cartier, L., Collados, L., Kettlun, A. M., Araya, F., Concha, C., Flores, L., Wolf, M. E., & Mosnaim, A. D. (1999). Gelatinase activity of matrix metalloproteinases in the cerebrospinal fluid of various patient populations. Research Communications in Molecular Pathology and Pharmacology, 104(1), 42-52.
Valenzuela MA, et al. Gelatinase Activity of Matrix Metalloproteinases in the Cerebrospinal Fluid of Various Patient Populations. Res Commun Mol Pathol Pharmacol. 1999;104(1):42-52. PubMed PMID: 10604277.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Gelatinase activity of matrix metalloproteinases in the cerebrospinal fluid of various patient populations. AU - Valenzuela,M A, AU - Cartier,L, AU - Collados,L, AU - Kettlun,A M, AU - Araya,F, AU - Concha,C, AU - Flores,L, AU - Wolf,M E, AU - Mosnaim,A D, PY - 1999/12/22/pubmed PY - 1999/12/22/medline PY - 1999/12/22/entrez SP - 42 EP - 52 JF - Research communications in molecular pathology and pharmacology JO - Res Commun Mol Pathol Pharmacol VL - 104 IS - 1 N2 - We have studied the enzymatic gelatinolytic activity of matrix metalloproteinases (MMPs) present in cerebrospinal fluid (CSF) of samples obtained from 67 individuals, twenty-one nonneurological patients (considered controls) and 46 subjects with various neurological disorders e.g., vascular lesions, demyelination, inflammatory, degenerative and prion diseases. Biochemical characterization of MMPs, a family of neutral proteolytic enzymes involved in extracellular matrix modeling, included determination of substrate specificity and Ca+2 dependency, as well as the effects of protease inactivators, carboxylic and His (histidine) residue modifiers, and antibiotics. Whereas all CSF samples expressed MMP-2 (gelatinase A) activity, it corresponded in most cases (normal and pathological samples) to its latent form (proenzyme; pMMP-2). In general, inflammatory neurological diseases (especially meningitis and neurocisticercosis) were associated with the presence of a second enzyme, MMP-9 (or gelatinase B). Whereas MMP-9 was found in the CSF of every tropical spastic paraparesis patient studied, its presence in samples from individuals with vascular lesions was uncommon. Patients blood-brain barrier damage was ascertained by determining total CSF protein content using both, the conventional polyacrylamide gel electrophoresis procedure under denaturing conditions and capillary zone electrophoresis. SN - 1078-0297 UR - https://www.unboundmedicine.com/medline/citation/10604277/Gelatinase_activity_of_matrix_metalloproteinases_in_the_cerebrospinal_fluid_of_various_patient_populations_ L2 - https://medlineplus.gov/neurologicdiseases.html DB - PRIME DP - Unbound Medicine ER -