Sandbox Reserved 468: Difference between revisions

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== Matrix Metalloproteinase-1 (MMP-1) ==

Matrix Metalloproteinase-1 (MMP-1)is interstitial collagenase and fibroblast collagenase. The enzyme in humans is encoded by the MMP1 gene. Human Fibroblast Collagenase (MMP-1) was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA.

Matrix Metalloproteinase-1 (MMP-1)is interstitial collagenase and fibroblast collagenase. The enzyme in humans is encoded by the MMP1 gene. Human Fibroblast Collagenase (MMP-1) was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA [1].

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. MMP-1, as with most MMP's, is secreted as inactive proproteins which is later activated when cleaved by extracellular proteases [2].

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. MMP-1, as with most MMP's, is secreted as inactive proproteins which is later activated when cleaved by extracellular proteases [2][3].

Most MMPs are secreted into the extracellular space as latent enzymes that are activated proteolytically by serine proteinases or by other MMPs. However, one intriguing sub-group of MMPs is the MT-MMPs, membrane-anchored MMPs that are activated intracellularly by a furin-like mechanism and inserted into the membrane in an active form. The first membrane-bound form, MT1-MMP, was described about 10 years ago, and this sub-group now contains six members. Their membrane-bound location appears to confer unique characteristics. Consequently, interest in their structure and function, their pattern of expression and the mechanisms regulating their expression and activity continues to grow [2].

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== Structure ==

The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by different protein building blocks. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene>, a Linker Region and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. The structure was determined by using X-ray crystallography and NMR. Two main names for the primary structure are currently in use, the original one from which the first amino-acid starts with the signaling peptide and a second one where the first amino-acid starts counting from the prodomain (this is known as the proenzyme nomenclature).

The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by different protein building blocks. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene>, a Linker Region and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. The structure was determined by using X-ray crystallography and NMR. Two main names for the primary structure are currently in use, the original one from which the first amino-acid starts with the signaling peptide and a second one where the first amino-acid starts counting from the prodomain (this is known as the proenzyme nomenclature) [2][3].

'''Catalytic Domain'''

The Catalytic Domains of all MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40Å. Despite the similarity of the Catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 Catalytic Domain. The <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role [2].

The Catalytic Domain (CAT) of MMP-1 starts with the F100 as the first amino-acid of the N-terminal loop of the CAT domain. This is different from the first published x-ray structure of the CAT domain was showed the truncated form of this domain, where the first 7 amino-acids are not present.

The Catalytic Domain (CAT) of MMP-1 starts with the F100 as the first amino-acid of the N-terminal loop of the CAT domain. This is different from the first published x-ray structure of the CAT domain was showed the truncated form of this domain, where the first 7 amino-acids are not present [6].

'''Linker region'''

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== Medical Implications ==

Research has shown that MMP-1 may have many medical implications. MMP-1 plays an important role in many physiologic processes such as development, tissue morphogenesis, wound repair and the remodeling of collagenous extracellular matrix. The enzyme is expressed by over 30 different cells. MMP-1 gene expression has also been shown to have implications with cancer treatment. MMP-1 can be used as a candidate marker that may be useful for identification of breast lesions that can develop into cancer.

Research has shown that MMP-1 may have many medical implications. MMP-1 plays an important role in many physiologic processes such as development, tissue morphogenesis, wound repair and the remodeling of collagenous extracellular matrix. The enzyme is expressed by over 30 different cells. MMP-1 gene expression has also been shown to have implications with cancer treatment. MMP-1 can be used as a candidate marker that may be useful for identification of breast lesions that can develop into cancer [5].

Sandbox Reserved 468: Difference between revisions

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@@ Line 5: / Line 5: @@
 == Matrix Metalloproteinase-1 (MMP-1) ==
-Matrix Metalloproteinase-1 (MMP-1)is interstitial collagenase and fibroblast collagenase. The enzyme in humans is encoded by the MMP1 gene. Human Fibroblast Collagenase (MMP-1) was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA.
+Matrix Metalloproteinase-1 (MMP-1)is interstitial collagenase and fibroblast collagenase. The enzyme in humans is encoded by the MMP1 gene. Human Fibroblast Collagenase (MMP-1) was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA [1].
-Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. MMP-1, as with most MMP's, is secreted as inactive proproteins which is later activated when cleaved by extracellular proteases [2].
+Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. MMP-1, as with most MMP's, is secreted as inactive proproteins which is later activated when cleaved by extracellular proteases [2][3].
 Most MMPs are secreted into the extracellular space as latent enzymes that are activated proteolytically by serine proteinases or by other MMPs. However, one intriguing sub-group of MMPs is the MT-MMPs, membrane-anchored MMPs that are activated intracellularly by a furin-like mechanism and inserted into the membrane in an active form. The first membrane-bound form, MT1-MMP, was described about 10 years ago, and this sub-group now contains six members. Their membrane-bound location appears to confer unique characteristics. Consequently, interest in their structure and function, their pattern of expression and the mechanisms regulating their expression and activity continues to grow [2].
@@ Line 13: / Line 13: @@
 == Structure ==
-The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by different protein building blocks. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene>, a Linker Region and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. The structure was determined by using X-ray crystallography and NMR. Two main names for the primary structure are currently in use, the original one from which the first amino-acid starts with the signaling peptide and a second one where the first amino-acid starts counting from the prodomain (this is known as the proenzyme nomenclature).
+The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by different protein building blocks. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene>, a Linker Region and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. The structure was determined by using X-ray crystallography and NMR. Two main names for the primary structure are currently in use, the original one from which the first amino-acid starts with the signaling peptide and a second one where the first amino-acid starts counting from the prodomain (this is known as the proenzyme nomenclature) [2][3].
 '''Catalytic Domain'''
 The Catalytic Domains of all MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40Å. Despite the similarity of the Catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 Catalytic Domain. The <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role [2].
-The Catalytic Domain (CAT) of MMP-1 starts with the F100 as the first amino-acid of the N-terminal loop of the CAT domain. This is different from the first published x-ray structure of the CAT domain was showed the truncated form of this domain, where the first 7 amino-acids are not present.
+The Catalytic Domain (CAT) of MMP-1 starts with the F100 as the first amino-acid of the N-terminal loop of the CAT domain. This is different from the first published x-ray structure of the CAT domain was showed the truncated form of this domain, where the first 7 amino-acids are not present [6].
 '''Linker region'''
@@ Line 43: / Line 43: @@
 == Medical Implications ==
-Research has shown that MMP-1 may have many medical implications. MMP-1 plays an important role in many physiologic processes such as development, tissue morphogenesis, wound repair and the remodeling of collagenous extracellular matrix. The enzyme is expressed by over 30 different cells. MMP-1 gene expression has also been shown to have implications with cancer treatment. MMP-1 can be used as a candidate marker that may be useful for identification of breast lesions that can develop into cancer.
+Research has shown that MMP-1 may have many medical implications. MMP-1 plays an important role in many physiologic processes such as development, tissue morphogenesis, wound repair and the remodeling of collagenous extracellular matrix. The enzyme is expressed by over 30 different cells. MMP-1 gene expression has also been shown to have implications with cancer treatment. MMP-1 can be used as a candidate marker that may be useful for identification of breast lesions that can develop into cancer [5].