{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,9]],"date-time":"2026-04-09T21:10:42Z","timestamp":1775769042963,"version":"3.50.1"},"reference-count":90,"publisher":"American Veterinary Medical Association (AVMA)","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["ajvr"],"published-print":{"date-parts":[[2009,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    <jats:bold>Objective<\/jats:bold>\n                    \u2014To measure the effects of lowmolecular-weight inhibitors on the activity of bovine neutrophil matrix metalloproteinase 9 (MMP-9).\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>Sample Population<\/jats:bold>\n                    \u2014Bovine MMP-9 purified from bovine neutrophilconditioned medium.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>Procedures<\/jats:bold>\n                    \u2014Neutrophils were degranulated by stimulation with phorbol ester. Enzyme purification was performed by use of gelatin affinity and gel-filtration chromatography. Activated enzyme was incubated with inhibitors prior to addition of substrate (gelatin fluorescein conjugate or fluorogenic peptide). Rates of enzymatic cleavage were determined by monitoring fluorescence as the reactions progressed. Values of IC\n                    <jats:sub>50<\/jats:sub>\n                    (molar concentration of compound that inhibits specific activity by 50%) and K\n                    <jats:sub>I<\/jats:sub>\n                    (in vitro inhibition constant) were determined.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>Results<\/jats:bold>\n                    \u2014Rates of enzymatic activity of monomeric and dimeric bovine MMP-9 measured by use of gelatin and peptide substrates were linear with respect to time and concentrations of enzyme and substrate. The MMP-9 was potently inhibited by hydroxamic acids (IC\n                    <jats:sub>50<\/jats:sub>\n                    for gelatin, 29.2 to 55.7nM; IC\n                    <jats:sub>50<\/jats:sub>\n                    for peptide, 4.8 to 24.6nM; K\n                    <jats:sub>I<\/jats:sub>\n                    , 0.2 to 0.5nM), whereas tetracyclines (IC\n                    <jats:sub>50<\/jats:sub>\n                    for gelatin, 30.1 to 112.7MM; IC\n                    <jats:sub>50<\/jats:sub>\n                    for peptide, 48.0 to 123.8MM; K\n                    <jats:sub>I<\/jats:sub>\n                    , 25.2 to 61.4\u00b5M) and chlorhexidine (IC\n                    <jats:sub>50<\/jats:sub>\n                    for gelatin, 139.1MM; IC\n                    <jats:sub>50<\/jats:sub>\n                    for peptide, 672.5MM to 1.7mM; K\n                    <jats:sub>I<\/jats:sub>\n                    , 495.0 to 663.0MM) had limited inhibition. Gelatinase-specific inhibitor SB-3CT had intermediate potency (IC\n                    <jats:sub>50<\/jats:sub>\n                    for peptide, 185.0 to 290.0nM; K\n                    <jats:sub>I<\/jats:sub>\n                    , 66.5 to 86.0nM).\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>Conclusions and Clinical Relevance<\/jats:bold>\n                    \u2014Bovine MMP-9 was potently inhibited by hydroxamic acids and gelatinase inhibitor. These compounds may be useful as modulators of neutrophil-mediated protease activity in cattle.\n                  <\/jats:p>","DOI":"10.2460\/ajvr.70.5.633","type":"journal-article","created":{"date-parts":[[2009,5,1]],"date-time":"2009-05-01T03:05:47Z","timestamp":1241147147000},"page":"633-639","source":"Crossref","is-referenced-by-count":3,"title":["Kinetics of inhibition of purified bovine neutrophil matrix metalloproteinase 9 by low\u2013molecular-weight inhibitors"],"prefix":"10.2460","volume":"70","author":[{"given":"Gregory A.","family":"Bannikov","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jeffrey","family":"Lakritz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christopher","family":"Premanandan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John S.","family":"Mattoon","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eric J.","family":"Abrahamsen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1272","reference":[{"key":"ref1","series-title":"Microbes Infect","doi-asserted-by":"publisher","first-page":"1079","DOI":"10.1016\/S1286-4579(00)01262-4","article-title":"Response of the ruminant respiratory tract to Mannheimia (Pasteurella) hemolytica","volume":"2","author":"Ackermann","year":"2000"},{"key":"ref2","series-title":"Vet Rec","doi-asserted-by":"publisher","first-page":"438","DOI":"10.1136\/vr.117.17.438","article-title":"Sequential lesions of experimental bovine pneumonic pasteurellosis","volume":"117","author":"Allan","year":"1985"},{"key":"ref3","series-title":"Am J Vet Res","first-page":"2253","article-title":"Importance of neutrophils in the pathogenesis of acute pneumonic pasteurellosis in calves","volume":"46","author":"Slocombe","year":"1985"},{"key":"ref4","series-title":"J Vet Intern Med","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1111\/j.1939-1676.1992.tb00980.x","article-title":"Pasteurella hemolytica A1 and bovine respiratory disease: pathogenesis","volume":"6","author":"Whiteley","year":"1992"},{"key":"ref5","series-title":"J Vet Intern Med","doi-asserted-by":"publisher","first-page":"516","DOI":"10.1111\/j.1939-1676.2001.tb01586.x","article-title":"Cell adhesion molecules, leukocyte trafficking, and strategies to reduce leukocyte infiltration","volume":"15","author":"Radi","year":"2001"},{"key":"ref6","series-title":"Free Radic Biol Med","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1016\/S0891-5849(02)00823-7","article-title":"Mediators and regulation of neutrophil accumulation in inflammatory responses in lung: insights from the IgG immune complex model","volume":"33","author":"Guo","year":"2002"},{"key":"ref7","series-title":"Nat Immunol","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1038\/ni773","article-title":"Decreased allergic lung inflammatory cell egression and increased susceptibility to asphyxiation in MMP2-deficiency","volume":"3","author":"Corry","year":"2002"},{"key":"ref8","series-title":"Vet Immunol Immunopathol","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1016\/S0165-2427(98)00228-1","article-title":"Secretion of 92 KDa gelatinase (MMP-9) by bovine neutrophils","volume":"67","author":"Li","year":"1999"},{"key":"ref9","series-title":"J Biol Chem","doi-asserted-by":"publisher","first-page":"11634","DOI":"10.1074\/jbc.271.20.11634","article-title":"Metalloproteinase-mediated regulation of L-selectin levels on leukocytes","volume":"271","author":"Preece","year":"1996"},{"key":"ref10","series-title":"J Biol Chem","doi-asserted-by":"publisher","first-page":"7019","DOI":"10.1074\/jbc.271.12.7019","article-title":"Shedding of the lymphocyte L-selectin adhesion molecule is inhibited by a hydroxamic acid-based protease inhibitor. 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Exp Biol Med","doi-asserted-by":"publisher","first-page":"863","DOI":"10.3181\/00379727-147-38457","article-title":"A procedure for granulokinetic investigation in the developing bovine using chromium 51","volume":"147","author":"Carlson","year":"1974"},{"key":"ref36","series-title":"Am J Vet Res","doi-asserted-by":"publisher","first-page":"163","DOI":"10.2460\/ajvr.2004.65.163","article-title":"Characterization of gelatinases in bronchoalveolar lavage fluid and gelatinases produced by alveolar macrophages isolated from healthy calves","volume":"65","author":"Lakritz","year":"2004"},{"key":"ref37","series-title":"J Biol Chem","doi-asserted-by":"publisher","first-page":"11201","DOI":"10.1074\/jbc.M111021200","article-title":"Design, synthesis and characterization of potent, slow-binding inhibitors that are selective for gelatinases","volume":"277","author":"Bernardo","year":"2002"},{"key":"ref38","series-title":"Bioorg Med 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Rec","doi-asserted-by":"publisher","first-page":"438","DOI":"10.1136\/vr.117.17.438","article-title":"Sequential lesions of experimental bovine pneumonic pasteurellosis","volume":"117","author":"Allan","year":"1985"},{"key":"ref3","series-title":"Am J Vet Res","first-page":"2253","article-title":"Importance of neutrophils in the pathogenesis of acute pneumonic pasteurellosis in calves","volume":"46","author":"Slocombe","year":"1985"},{"key":"ref4","series-title":"J Vet Intern Med","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1111\/j.1939-1676.1992.tb00980.x","article-title":"Pasteurella hemolytica A1 and bovine respiratory disease: pathogenesis","volume":"6","author":"Whiteley","year":"1992"},{"key":"ref5","series-title":"J Vet Intern Med","doi-asserted-by":"publisher","first-page":"516","DOI":"10.1111\/j.1939-1676.2001.tb01586.x","article-title":"Cell adhesion molecules, leukocyte trafficking, and strategies to reduce leukocyte 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