Serum levels and tissue expression of matrix metalloproteinase 2 (MMP-2) and tissue inhibitor of metalloproteinases 2 (TIMP-2) in colorectal cancer patients

Aim. To study the level of matrix metalloproteinases-1 and -2, and tissue inhibitor of metalloproteinases-1, the indicator of left ventricular myocardial deformation in patients with stage 12 hypertension. Methods. 114 patients (40 women and 74 men) with hypertension of 12 stages observed in the cardiology Department of the Road clinical hospital Chita II were examined. The median age was 428.3 years. Left ventriclular diastolic function was studied by using tissue Doppler imaging in apical four-chamber views. Serum matrix metalloproteinase-1, matrix metalloproteinase-2, and tissue inhibitor of metalloproteinases-1 levels were measured in all patients on automated immunoassay analyzers using ready-to-use ELISA kits. Results. An increase in serum levels of matrix metalloproteinases-1 and -2 in the group of patients with hypertension and diastolic dysfunction by 46 and 47%, respectively, was found against increased levels of serum tissue inhibitor of metalloproteinase-1 (р=0.049). In patients with diastole dysfunction, myocardial global longitudinal strain was decreased in was observed by 22.8% compared with patients without diastole dysfunction (p 0.05). The analysis revealed a moderate negative relationship between left ventricular global longitudinal strain and the serum levels of metalloproteinases-2 (r=0.64, p 0.05). Conclusion. In patients with hypertension and left ventricular diastolic dysfunction, a decrease in left ventricular global longitudinal strain is associated with the serum level of matrix metalloproteinase-2; a tissue inhibitor of metalloproteinases-1 is unrelated to left ventricular global myocardial strain.

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Postoperative Serum Levels of sCD26 for Surveillance in Colorectal Cancer Patients

PLoS ONE ◽

10.1371/journal.pone.0107470 ◽

2014 ◽

Vol 9 (9) ◽

pp. e107470 ◽

Cited By ~ 10

Author(s):

Loretta De Chiara ◽

Ana M. Rodríguez-Piñeiro ◽

Oscar J. Cordero ◽

Lidia Vázquez-Tuñas ◽

Daniel Ayude ◽

...

Keyword(s):

Colorectal Cancer ◽

Cancer Patients ◽

Serum Levels ◽

Postoperative Serum ◽

Colorectal Cancer Patients

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Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate

Biochemical Journal ◽

10.1042/bj3080645 ◽

1995 ◽

Vol 308 (2) ◽

pp. 645-651 ◽

Cited By ~ 70

Author(s):

Y Itoh ◽

S Binner ◽

H Nagase

Keyword(s):

Matrix Metalloproteinase ◽

Noncovalent Complex ◽

The Other ◽

Gelatinolytic Activity ◽

Matrix Metalloproteinase 2 ◽

Tissue Inhibitor Of Metalloproteinases ◽

Tissue Inhibitor ◽

Sh Group ◽

Inhibitory Domain ◽

Interstitial Collagenase

Tissue inhibitor of metalloproteinases (TIMP)-2 forms a noncovalent complex with the precursor of matrix metalloproteinase 2 (proMMP-2, progelatinase A) through interaction of the C-terminal domain of each molecule. We have isolated the proMMP-2-TIMP-2 complex from the medium of human uterine cervical fibroblasts and investigated the processes involved in its activation by 4-aminophenylmercuric acetate (APMA). The treatment of the complex with APMA-activated proMMP-2 by disrupting the Cys73-Zn2+ interaction of the zymogen. This is triggered by perturbation of the proMMP-2 molecule, but not by the reaction of the SH group of Cys73 with APMA. The ‘activated’ proMMP-2 (proMMP-2*) formed a new complex with TIMP-2 by binding to the N-terminal inhibitory domain of the inhibitor without processing the propeptide. Thus the APMA-treated proMMP-2*-TIMP-2 complex exhibited no gelatinolytic activity. In the presence of a small amount of free MMP-2, however, proMMP-2* in the complex was converted into the 65 kDa MMP-2 by proteolytic attack of MMP-2, but the complex did not exhibit gelatinolytic activity. The gelatinolytic activity detected after APMA treatment was solely derived from the activation of free proMMP-2. The removal of the propeptide of the proMMP-2* bound to TIMP-2 was also observed by MMP-3 (stromelysin 1), but not by MMP-1 (interstitial collagenase). MMP-3 cleaved the Asn80-Tyr81 bond of proMMP-2*. On the other hand, when MMP-3 was incubated with the proMMP-2-TIMP-2 complex, it bound to TIMP-2 and rendered proMMP-2 readily activatable by APMA. These results indicate that the blockage of TIMP-2 of the complex with an active MMP is essential for the activation of proMMP-2 when it is complexed with TIMP-2.

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Composition and Concentration of Serum Fatty Acids of Phospholipids Depend on Tumour Location and Disease Progression in Colorectal Patients

Journal of Medical Biochemistry ◽

10.1515/jomb-2017-0031 ◽

2018 ◽

Vol 37 (1) ◽

pp. 39-45 ◽

Cited By ~ 3

Author(s):

Jolanta Bugajska ◽

Joanna Berska ◽

Diana Hodorowicz-Zaniewska ◽

Krystyna Sztefko

Keyword(s):

Colorectal Cancer ◽

Fatty Acids ◽

Disease Progression ◽

Cancer Patients ◽

Distal Colon ◽

Unsaturation Index ◽

Serum Levels ◽

Colorectal Tumour ◽

Tumour Localization ◽

Colorectal Cancer Patients

SummaryBackground: Polyunsaturated fatty acids (PUFAs) play a role in the development/progression of colon cancer. The aim of the study was to assess the relation between serum phospholipids PUFAs, colorectal tumour localization and disease progression. Methods: A total of 67 patients (18 with proximal colon, 17 with distal colon and 32 with rectal tumour localization) as well as 16 controls were studied. One year after surgery, 33 patients had disease progression. Serum levels of C16:1(n-7), C18:1(n-9), C18:3(n-3), C20:5(n-3), C22:6(n- 3), C18:2(n-6), C20:2(n-6), C20:4(n-6) fatty acids of se - rum phospholipids were quantitatively measured before surgery by gas-chromatography. Results: Significantly higher mean value of C18:2, as compared to control, has been noted only for patients with proximal (p<0.05) and distal tumour (p<0.03) localization. The lower mean level of C20:5 and unsaturation index (UI) were observed in colorectal cancer patients regardless the tumour localization, but the statistical difference was noted only for patients with proximal tumours (p<0.05, p<0.03). In patients with proximal tumours, significantly lower mean level of C20:4 and UI were noted in patients with disease progression, as compared to patients with proximal tumours without disease progression (p<0.05). Conclusion: The evaluation of PUFAs as a risk/prognostic factor in colorectal cancer patients should take into account tumour localization as a dependent variable.

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Serum levels of tissue factor in colorectal cancer patients

International Journal of Clinical Oncology ◽

10.1007/bf02628048 ◽

1998 ◽

Vol 3 (5) ◽

pp. 287-290

Author(s):

Chika Shigemori

Keyword(s):

Colorectal Cancer ◽

Cancer Patients ◽

Tissue Factor ◽

Serum Levels ◽

Colorectal Cancer Patients

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KCNB1 gene polymorphisms and related indel as predictor biomarkers of treatment response for colorectal cancer – toward a personalized medicine

Tumor Biology ◽

10.1177/1010428320925237 ◽

2020 ◽

Vol 42 (6) ◽

pp. 101042832092523 ◽

Cited By ~ 2

Author(s):

Mouadh Barbirou ◽

Ikram Sghaier ◽

Sinda Bedoui ◽

Rahma Ben Abderrazek ◽

Hazar Kraiem ◽

...

Keyword(s):

Colorectal Cancer ◽

Treatment Response ◽

Cancer Patients ◽

Serum Levels ◽

Amplification Refractory Mutation System ◽

Specific Response ◽

Tumor Localization ◽

Gene Variants ◽

Treatment And Prevention ◽

Colorectal Cancer Patients

The KCNB1 gene variants were differentially associated with cancers. However, their association with colorectal cancer has not yet been explored. We investigated the contribution of the KCNB1 gene variants rs3331, rs1051295, and indel (insertion/deletion) rs11468831 Polymorphism as predictors of the treatment response in colorectal cancer patients. A retrospective study, which involved 291 Tunisian colorectal cancer patients (aged 60.0 ± 13.1 years), who were stratified into responder and non-responder groups, according to TNM stages and their responsiveness to chemotherapy based on fluorouracil. KCNB1 genotyping was performed with amplification-refractory mutation system–polymerase chain reaction, and was confirmed by Sanger sequencing. Sex-specific response was found and colorectal cancer females are less likely to achieve a positive response during the chemotherapy strategy, compared to males. Weight and body mass index, tumor size, and tumor localization are considered as predictive factors to treatment responsiveness. Carriage of rs11468831 Ins allele was significantly associated with successful therapy achievement ( p adjusted < 0.001). Stratification of colorectal cancer patients’ response according to tumor localization and TNM stages reveals negative association of rs3331 Major allele to treatment response among the patients with advanced cancer stages (subgroup G2). The presence of rs3331 (homozygous minor) C/C genotype was positively associated with decline in carcino-embryonic antigen ( p = 0.043) and CA19-9 ( p = 0.014) serum levels. On the other hand, the presence of rs1051295 (homozygous minor) A/A genotype was correlated with marked decline in CA19-9 serum levels. KCNB1 haplotype did not reveal any association between haplotypes and treatment response. The results obtained suggest that gender-specific strategies for screening treatment and prevention protocols as well as KCNB1 variants may constitute an effective model for ongoing personalization medicine.

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