Search Results

You are looking at 1 - 3 of 3 items for

  • Author or Editor: Kara C. Sorensen x
  • Refine by Access: All Content x
Clear All Modify Search

Abstract

Objective—To screen for expression of 9 predominant members of the matrix metalloproteinase (MMP) family, including membrane-type matrix metalloproteinases (MT-MMPs) and tissue inhibitors of metalloproteinases (TIMPs), in primary tumor tissue biopsy specimens of vaccine site-associated sarcomas (VSS) in cats and compare expression profiles of VSS with expression profiles of non-VSS and carcinomas.

Sample Population—31 primary tumor tissue biopsy specimens and 6 nontumor (normal) tissue biopsy specimens.

Procedure—Tissue specimens were obtained from primary tumor biopsy specimens of cats. Primers for reverse transcriptase-polymerase chain reaction assay were designed on the basis of known sequences. Data were analyzed for patterns of expression of MMPs, MT-MMPs, and TIMPs. Differences in expression patterns were evaluated among cats of differing genders, ages, metastasis status, and overall survival durations, and between cats with VSS and cats with non-VSS tumor types.

Results—A total of 31 primary tumor tissue biopsy specimens and 6 nontumor (normal) tissue biopsy specimens were screened for the presence of 6 MMPs and 3 TIMPs. Matrix metalloproteinase and TIMP expression was found in non-VSS, carcinomas, and VSS. No significant differences were found in patterns of expression among tumor types. Metastasis was found to be the only predictive factor for overall survival duration. A significant correlation was found between MMP2 and MT-MMP16 expression and overall duration of survival.

Conclusions and Clinical Relevance—The identification of MMPs in feline VSS supports an underlying inflammatory pathogenesis for this tumor. Expression of MMP2 and MT-MMP16 were correlated with survival time in our study. ( Am J Vet Res 2004; 65:373–379)

Full access
in American Journal of Veterinary Research

Abstract

Objective—To detect, isolate, and characterize feline stromelysin-1 (ie, matrix metalloproteinase [MMP]-3) in naturally developing tumors in cats.

Sample Population—31 tissue samples obtained from primary tumors and 6 samples of normal tissues from cats.

Procedure—Biopsy specimens were obtained from primary tumors. Primers were designed on the basis of known sequences. The sequence of stromelysin- 1 was cloned and analyzed. An additional primer set was used as a screening tool. Samples were assayed in duplicate or triplicate, when possible. Data obtained were analyzed for differences in expression of stromelysin-1 with regard to overall survival among cats of various sex, age, and disease status.

Results—A 1,181-bp cDNA nucleotide sequence was amplified. The open reading frame encoded 393 amino acids. This amino acid sequence shared 70% to 85% sequence homology with sequences of other species. In addition, samples were screened for stromelysin-1. Of the 31 tumor samples tested, 16 (51.6%) had positive results for expression of stromelysin-1. Total RNA expression was detected in a diverse group of tumor types. Prognostic factors associated with a shorter duration of survival included evidence of metastasis and metastasis associated with expression of stromelysin-1.

Conclusions and Clinical Relevance—Feline stromelysin-1 contains all the conserved regions typically found in members of the MMP family. Activity of stromelysin-1 has been implicated in a wide number of physiologic and pathologic processes. Identification of this gene may lead to the development of useful reagents to assist with diagnosis and management of neoplastic diseases in cats. (Am J Vet Res 2004; 65:213–219)

Full access
in American Journal of Veterinary Research

Abstract

Objective—To isolate and characterize the cDNA sequence of canine stromelysin-1 (matrix metalloproteinase [MMP]-3), screen various naturally developing primary tumors of dogs, and assess the effect of stromelysin-1 on survival of dogs with cancer.

Sample Population—3 canine cell lines and biopsy specimens of primary tumors collected from 54 dogs.

Procedure—3 canine cell lines and biopsy specimens of primary tumors collected from 54 dogs at the University of Illinois Veterinary Teaching Hospital were used in the study. Primer sets based on human stromelysin-1 and consensus sequences were designed for expression, screening, and isolation. Two additional primer sets were designed for screening. Samples were assayed at least in duplicate. Data were analyzed for differences in expression of stromelysin-1 on the basis of sex, age, metastasis, malignant versus nonmalignant tissue origin, and duration of patient survival.

Results—A 1,479-bp cDNA nucleotide sequence was amplified from established canine cell lines. The open reading frame encoded a protein consisting of 478 amino acids. This sequence was 70% to 88% homologous with stromelysin-1 of other species at the amino acid level. Fifty-four samples were screened for stromelysin-1. Of these, 34 (63%) had positive results and 20 (37%) had negative results for expression. Stromelysin-1 and metastasis were associated with a poor prognosis for survival.

Conclusions and Clinical Relevance—Stromelysin-1 is a potential activator of other members of the MMP family. Additional studies are needed to investigate the relationship between stromelysin-1 production and aggressive biological behavior of tumors in dogs. (Am J Vet Res 2005;66:1526–1535)

Full access
in American Journal of Veterinary Research