Biomedical subjects

Mary Ann Kosir

Publications and source records attributed to Mary Ann Kosir.

4 recordsLinked to original sources

PubMed2004

Murine ocular heparanase expression before and during infection with Pseudomonas aeruginosa.

PURPOSE: To demonstrate the constitutive expression and regulation of heparanase (heparan sulfate endoglycosidase) in the normal mouse eye and in mice intracorneally infected with Pseudomonas aeruginosa. METHODS: Naïve (unimmunized) and immunized C57BL/6J mice were infected with P. aeruginosa, and corneal heparanase gene and protein expression were detected by semiquantitative RT-PCR and immunoblot analysis. Immunohistochemistry was also applied to characterize corneal heparanase in naïve mice. RESULTS: Heparanase mRNA and protein expression were detected in uninfected corneas of C57BL/6J mice. Immunohistochemical studies indicated heparanase protein expression was primarily in the corneal epithelium before corneal infection and was also in the corneal stroma after infection. Immunohistochemical studies of uninfected and infected whole eyes of naïve mice indicated heparanase protein expression in most layers of the retina, but the expression did not appear to be upregulated during corneal infection. Staining was most intense in the inner photoreceptor layer of the retina. CONCLUSIONS: Heparanase was constitutively expressed in both the corneal epithelium and several retinal layers before intracorneal infection with P. aeruginosa. Temporal upregulation of corneal heparanase protein expression was detected in naïve mice during infection, most likely due to heparanase positive infiltrating cells, but the protein was not upregulated in corneas from immunized mice because they had a lower inflammatory response, associated with the restoration of corneal clarity. There did not appear to be temporal upregulation of heparanase expression in the retina of infected mice, as determined by immunohistochemistry.

Animals↗

PubMed2003

Can a practicing surgeon detect early lymphedema reliably?

BACKGROUND: Lymphedema may be identified by simpler circumference changes as compared with changes in limb volume. METHODS: Ninety breast cancer patients were prospectively enrolled in an academic trial, and seven upper extremity circumferences were measured quarterly for 3 years. A 10% volume increase or greater than 1 cm increase in arm circumference identified lymphedema with verification by a lymphedema specialist. Sensitivity and specificity of several different criteria for detecting lymphedema were compared using the academic trial as the standard. RESULTS: Thirty-nine cases of lymphedema were identified by the academic trial. Using a 10% increase in circumference at two sites as the criterion, half the lymphedema cases were detected (sensitivity 37%). When using a 10% increase in circumference at any site, 74.4% of cases were detected (sensitivity 49%). Detection by a 5% increase in circumference at any site was 91% sensitive. CONCLUSIONS: An increase of 5% in circumference measurements identified the most potential lymphedema cases compared with an academic trial.

Arm↗

PubMed2002

Ethnicity related differences in the survival of young breast carcinoma patients.

BACKGROUND: African-American women face an increased risk of early-onset breast carcinoma compared to white American women, and breast carcinoma has been reported to be particularly aggressive in premenopausal women. METHODS: Surveillance, Epidemiology, and End Results Program data were analyzed for 507 African-American and 1378 white patients from Detroit diagnosed with breast carcinoma under the age of 40 between 1990 and 1999. RESULTS: The proportion of in situ disease detected in African-American patients between 1995 and 1999 nearly doubled compared to the 1990-1994 interval (11.3% compared to 6.4%) but was consistently lower than the proportion of in situ disease seen in white patients for the same intervals (15.7% and 16.4% respectively). Evaluation of patients with invasive disease revealed that African-American patients had larger mean tumor size (3.4 cm versus 2.6 cm; P < 0.001), lower rates of localized disease (42.4% versus 52.1%; P < 0.001), higher rates of estrogen receptor negativity (61.9% versus 44.4%; P < 0.001), and higher proportions of medullary tumors (5.8% versus 3.3%; P = 0.021). Cox proportional hazards survival analysis adjusted for age, tumor size, nodal status, hormone receptor status, and histology showed higher mortality rates for African-American patients at all disease stages. Relative risk of death for African-American patients was 1.94 in patients with localized disease (95% confidence interval [CI], 1.23-3.05), 1.58 for regional disease (95% CI = 1.18-2.11), and 2.32 for distant disease (95% CI = 1.15-4.69). CONCLUSIONS: These findings show that young African-American breast carcinoma patients face an increased mortality risk. Additional studies evaluating risk and treatment response in this subset of patients are warranted.

Adult↗

PubMed2002

Multiple heparanases are expressed in polymorphonuclear cells.

BACKGROUND: Heparan sulfate proteoglycans are complex cell surface molecules containing polysaccharides called heparan sulfate. Lysosomes, platelet granules, and neutrophils (polymorphonuclear cells) contain heparanases that degrade heparan sulfate. There are at least two groups of heparanases: connective tissue-activating-peptide (CTAP-III) and mammalian heparanase (hpa). The purpose of this study was to quantify the expression of both CTAP-III and hpa in neutrophils and their heparanase activity. MATERIALS AND METHODS: Neutrophils were isolated from whole blood, total RNA collected, and reverse transcriptase--polymerase chain reaction (RT-PCR) performed. Primers were designed for CTAP-III and hpa-1 sequences from GenBank. Neutrophil lysate underwent Western blot analysis (and quantification) with antibodies to the C-terminus of CTAP-III and the 50-kDa subunit of hpa1. Chromatography separated these components of lysate, which were then tested for heparanase activity. RESULTS: Both CTAP-III (281 bp) and hpa-1 (485 bp) messenger RNA (mRNA) were expressed equally by neutrophils with use of quantitative RT-PCR. By Western blot analysis, a CTAP-III-like protein was detected at 80 kDa, and hpa-1 was detected as a 50-kDa protein, with expression not significantly different (P > 0.05). Heparanase activity was significantly different (P < 0.0001) for the 50-kDa hpa-1 protein (1.51 x 10(-6) micromol/min) and the 80-kDa CTAP-III-like protein (0.85 x 10(-6) micromol/min). CONCLUSIONS: Human neutrophils express mRNA and protein for both a CTAP-III-like protein and hpa-1. Although expressed in similar quantity for mRNA and protein, Hpa-1 was more active as heparanase than the CTAP-III-like protein. With more than one class of heparanase in their granules, neutrophils may be able to modify different kinds of heparan sulfate chains.

Amino Acid Sequence↗