Limits...
Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases.

Jaiswal A, Chhabra A, Malhotra U, Kohli S, Rani V - Bioinformation (2011)

Bottom Line: This initial screening can help to reduce time and cost of testing and experimentation in laboratory.Thus, a plausible grouping of disease responsive MMPs that might be considered as promising clinical targets may be done.This study can be used as a fundamental approach to characterize, analyze and screen large protein families for the identification of signature patterns.

View Article: PubMed Central - PubMed

Affiliation: Department of Biotechnology, Jaypee Institute of Information Technology, A-10, Sector-62, NOIDA- 201307, Uttar Pradesh, India.

ABSTRACT
The identification of specific target proteins for any diseased condition involves extensive characterization of the potentially involved proteins. Members of a protein family demonstrating comparable features may show certain unusual features when implicated in a pathological condition. Advancements in the field of computational biology and the use of various bioinformatics tools for analysis can aid researchers to comprehend their system of work in primary stages of research. This initial screening can help to reduce time and cost of testing and experimentation in laboratory. Human matrix metalloproteinase (MMP) family of endopeptidases is one such family of 23 members responsible for the remodeling of extracellular matrix (ECM) by degradation of the ECM proteins. Though their role has been implicated in various pathological conditions such as arthritis, atherosclerosis, cancer, liver fibrosis, cardio-vascular and neurodegenerative disorders, little is known about the specific involvement of members of the large MMP family in diseases. A comparative in silico characterization of the MMP protein family has been carried out to analyze their physico-chemical, secondary structural and functional properties. Based on the observed patterns of occurrence of atypical features, we hypothesize that cysteine rich and highly thermostable MMPs might be key players in diseased conditions. Thus, a plausible grouping of disease responsive MMPs that might be considered as promising clinical targets may be done. This study can be used as a fundamental approach to characterize, analyze and screen large protein families for the identification of signature patterns.

No MeSH data available.


Related in: MedlinePlus

Percentage of cysteine residues in human MMPs computed byExPASy's ProtParam tool. The amino acid composition of the 23 humanMMPs was analyzed. Cysteine showed an abnormal trend as the percentage ofcysteine residues in MMP-2, 9 and 23 was found to be exceptionally high ascompared to other MMPs.
© Copyright Policy - open-access
Related In: Results  -  Collection


getmorefigures.php?uid=PMC3064848&req=5

Figure 1: Percentage of cysteine residues in human MMPs computed byExPASy's ProtParam tool. The amino acid composition of the 23 humanMMPs was analyzed. Cysteine showed an abnormal trend as the percentage ofcysteine residues in MMP-2, 9 and 23 was found to be exceptionally high ascompared to other MMPs.

Mentions: Analysis of amino acid composition indicates that while the percentage ofcysteine residues in majority of MMPs lies in the range of 0.6-1.3%, MMP-2, 9and 23 show a significant rise with values 2.9, 2.7 and 2.8 percent, respectively(Figure 1) (See Table 2 insupplementary material). High percentage ofcysteine residues in MMP-2 and 9 might be correlated with presence ofcysteine switch motif and role of these MMPs in pathological conditions. Thesegelatinases have been previously implicated in carcinomas and cardio-vasculardisorders. High cysteine content of the unclassified MMP-23 might beattributed to the presence of cysteine array in its structure. Highly significantpresence of cysteine suggests its role as a critical residue for MMP activity andthus these MMPs may be investigated for possible role in diseased conditions.Further analysis of the amino acid composition can help to locate amino acidpresence at an unusual level and be correlated with specific pathologicalconditions [14].


Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases.

Jaiswal A, Chhabra A, Malhotra U, Kohli S, Rani V - Bioinformation (2011)

Percentage of cysteine residues in human MMPs computed byExPASy's ProtParam tool. The amino acid composition of the 23 humanMMPs was analyzed. Cysteine showed an abnormal trend as the percentage ofcysteine residues in MMP-2, 9 and 23 was found to be exceptionally high ascompared to other MMPs.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3064848&req=5

Figure 1: Percentage of cysteine residues in human MMPs computed byExPASy's ProtParam tool. The amino acid composition of the 23 humanMMPs was analyzed. Cysteine showed an abnormal trend as the percentage ofcysteine residues in MMP-2, 9 and 23 was found to be exceptionally high ascompared to other MMPs.
Mentions: Analysis of amino acid composition indicates that while the percentage ofcysteine residues in majority of MMPs lies in the range of 0.6-1.3%, MMP-2, 9and 23 show a significant rise with values 2.9, 2.7 and 2.8 percent, respectively(Figure 1) (See Table 2 insupplementary material). High percentage ofcysteine residues in MMP-2 and 9 might be correlated with presence ofcysteine switch motif and role of these MMPs in pathological conditions. Thesegelatinases have been previously implicated in carcinomas and cardio-vasculardisorders. High cysteine content of the unclassified MMP-23 might beattributed to the presence of cysteine array in its structure. Highly significantpresence of cysteine suggests its role as a critical residue for MMP activity andthus these MMPs may be investigated for possible role in diseased conditions.Further analysis of the amino acid composition can help to locate amino acidpresence at an unusual level and be correlated with specific pathologicalconditions [14].

Bottom Line: This initial screening can help to reduce time and cost of testing and experimentation in laboratory.Thus, a plausible grouping of disease responsive MMPs that might be considered as promising clinical targets may be done.This study can be used as a fundamental approach to characterize, analyze and screen large protein families for the identification of signature patterns.

View Article: PubMed Central - PubMed

Affiliation: Department of Biotechnology, Jaypee Institute of Information Technology, A-10, Sector-62, NOIDA- 201307, Uttar Pradesh, India.

ABSTRACT
The identification of specific target proteins for any diseased condition involves extensive characterization of the potentially involved proteins. Members of a protein family demonstrating comparable features may show certain unusual features when implicated in a pathological condition. Advancements in the field of computational biology and the use of various bioinformatics tools for analysis can aid researchers to comprehend their system of work in primary stages of research. This initial screening can help to reduce time and cost of testing and experimentation in laboratory. Human matrix metalloproteinase (MMP) family of endopeptidases is one such family of 23 members responsible for the remodeling of extracellular matrix (ECM) by degradation of the ECM proteins. Though their role has been implicated in various pathological conditions such as arthritis, atherosclerosis, cancer, liver fibrosis, cardio-vascular and neurodegenerative disorders, little is known about the specific involvement of members of the large MMP family in diseases. A comparative in silico characterization of the MMP protein family has been carried out to analyze their physico-chemical, secondary structural and functional properties. Based on the observed patterns of occurrence of atypical features, we hypothesize that cysteine rich and highly thermostable MMPs might be key players in diseased conditions. Thus, a plausible grouping of disease responsive MMPs that might be considered as promising clinical targets may be done. This study can be used as a fundamental approach to characterize, analyze and screen large protein families for the identification of signature patterns.

No MeSH data available.


Related in: MedlinePlus