Matrix Metalloproteinases-1, -3, and -8 in Adult Periodontitis in Situ.

Although prostate cancer (PCa) is the sixth most common type of neoplasm in the world and the second in prevalence among men (10% of all cases), there is shortage of studies focused on primary prevention of the disorder as well as little understanding on its pathophysiology. Currently, the PCa screening tools are the prostate specific antigen (PSA) dosage conjugated to rectal examination and confirmed by prostate biopsy. Despite the name, the PSA presents reduced specificity, being necessary the identification of new biomarkers that allow an earlier and more precise diagnosis and even better prognosis. Several studies have associated matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) to PCa tumorigenesis and metastasis. Most of the studies so far have been carried out by investigating in situ expression of the metalloproteinases, either by transcriptional measures or by immunohistochemistry with biopsy or postoperative tissue. Investigations in human plasma and serum are scarce, and a bibliographical search resulted in 17 studies which are presented and interpreted herein. This narrative review discusses their settings and findings along with aspects related to circulating metalloproteinases as potential biomarkers for diagnosis or prognosis of the prostatic malignancy, expressing the authors' reticent view on their applicability due to the poor quality of evidence available.

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244. Effect of batimastat, a specific inhibitor of matrix metalloproteinases, on endometrial breakdown and repair in a mouse model

Reproduction Fertility and Development ◽

10.1071/srb05abs244 ◽

2005 ◽

Vol 17 (9) ◽

pp. 97

Author(s):

T. J. Kaitu'u ◽

N. B. Morison ◽

L. A. Salamonsen

Keyword(s):

Matrix Metalloproteinases ◽

Mouse Model ◽

Expression Patterns ◽

Specific Inhibitor ◽

Apparent Difference ◽

Cross Sectional ◽

Gelatinase Activity ◽

Expected Time ◽

Mmp Inhibitor

Strong correlative evidence supports a role for matrix metalloproteinases (MMPs) in the tissue breakdown at menstruation. As menstruation occurs in very few species besides women, there is a lack of suitable and easily accessible animal models available to examine the functional significance of potential key mediators of this process. A mouse model of endometrial breakdown and repair has been developed,1 which morphologically resembles that of human endometrium at menstruation. Previous studies in our laboratory showed that the expression patterns of various MMPs in the mouse model closely resembled those seen in the human.2 Administration of doxycycline, a broad spectrum MMP inhibitor, decreased gelatinase activity, but had no effect on tissue breakdown in this model. The aim of the present study was to further examine the importance of MMPs in endometrial breakdown and repair via administration of batimistat, a highly potent and specific MMP inhibitor. Batimistat was administered I.P to mice 24 h prior to the expected time of endometrial breakdown. The efficacy of batimistat within the uterus was proven using in situ zymography, which identifies MMP activity (rather than latent forms). This demonstrated that batimistat was reaching its target organ and effectively inhibiting MMP activities (both gelatinase and collagenase). Examination of gross uterine morphology revealed no apparent difference between groups, with batimistat treated uteri displaying a similar extent of tissue breakdown and repair to their control counterparts. Measurement of the breaking down area compared to total endometrial area revealed no difference between control and batimistat treatment, with the breaking down areas being 69 ±13% and 72 ± 9.8% of total endometrial cross-sectional area respectively. There was likewise no effect on endometrial repair. The results of this study together with our previous study using doxycycline, indicate that MMPs are not the key mediators of endometrial breakdown in this model. (1)Shen et al. (2004) Reprod. Fert. Dev. 16(Suppl), A265, p. 97.(2)Brasted et al. (2003) Biol. Reprod. 69, 1273.

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In Situ AP/MALDI-MS characterization of anchored matrix metalloproteinases

Journal of Mass Spectrometry ◽

10.1002/jms.1126 ◽

2006 ◽

Vol 41 (12) ◽

pp. 1561-1569 ◽

Cited By ~ 25

Author(s):

Giuseppe Grasso ◽

Marco Fragai ◽

Enrico Rizzarelli ◽

Giuseppe Spoto ◽

Kwon Joo Yeo

Keyword(s):

Matrix Metalloproteinases ◽

Maldi Ms

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Faculty Opinions recommendation of Decidual leucocytes infiltrating human spiral arterioles are rich source of matrix metalloproteinases and degrade extracellular matrix in vitro and in situ.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.734102261.793561746 ◽

2019 ◽

Author(s):

Gendie Lash

Keyword(s):

Extracellular Matrix ◽

Matrix Metalloproteinases ◽

Rich Source

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Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

Biochemical Journal ◽

10.1042/bj2950595 ◽

1993 ◽

Vol 295 (2) ◽

pp. 595-598 ◽

Cited By ~ 78

Author(s):

Q Nguyen ◽

G Murphy ◽

C E Hughes ◽

J S Mort ◽

P J Roughley

Keyword(s):

Matrix Metalloproteinases ◽

Degradation Products ◽

Limited Proteolysis ◽

Human Cartilage ◽

Link Protein ◽

Sequencing Studies ◽

Proteoglycan Aggregates ◽

Protein Components ◽

Gelatinases A And B

The actions of human recombinant stromelysins-1 and -2, collagenase, gelatinases A and B and matrilysin on neonatal human proteoglycan aggregates were examined. With the exception of gelatinase B, aggrecan was degraded extensively by most metalloproteinases studied, whereas link protein showed only limited proteolysis. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Cleavage at the former bond generated a link protein component with the same N-terminus as that isolated from newborn human cartilage. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix.

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