| 總結: | Bovine collagen alpha-1 is a naturally occurring extracellular matrix protein found in tendons and other connective tissues. It plays
a vital role in cell growth, differentiation, attachment, and migration. Recent findings have established that collagen alpha-1 is
involved in osteogenesis imperfecta phenotype in cattle but deep information about other members of this large family is not
available so far. So with a view to finding a new edge and attempt to figure out a correlation among the well attributed Bovine
alpha-1 collagen sequences are executed and analyzed. To do so, comparative analysis among the 28 members of collagen family
has been carried out using Computational tools. Consequently, based on the physico-chemical, secondary structural, functional
and phylogenetic classifications, we have selected collagen 12, 14 and 20 as targets for pathological conditions. These proteins
belong to the FACIT family and significantly showed low glycine and proline content, high instability and aliphatic index.
Moreover, FACIT family collagens contain multiple triple helical domains and being members of the FACIT family, bovine
collagen 12, 14, 20 do not form fibrils by themselves but they are associated to collagen 1 associated fibrils. These collagen
molecules might be crucial candidates to detect and understand the process of matrix remodeling in diseases especially in the arena
of cellular compartments.
Collagen is the most abundant family of fibrous proteins in
mammals which is secreted by the connective tissue cells [1]. To
note about its localization, it is found mostly in flesh and
connective tissues in vertebrates [2]. Collagen structure is a
triple helix with three different chains and these three alpha
chains are wound around one another to form the superhelix
structure which gives the long, stiff structure of collagen protein
[3]. The amino acids in collagen are arranged in such a manner
that glycine is present in every third residue [4]. Glycine is the
smallest amino acid and thus fits perfectly in the helix and
allows the alpha chains to wrap around together to form the
superhelix. Collagen is rich in glycine and proline residues. So,
other than glycine in every third residue, the remaining two
amino acids are mostly occupied by proline. Pro-collagens are
inactive precursors of collagens. During the synthesis of
collagen, pro-collagens are synthesized at first. The mature
active collagen molecules are formed by the action of
peptidases cleaving the pro-peptides at the N and C terminals.
Vitamin C acts as a cofactor in conversion of pro-collagens to
collagens. Pro-collagens are cleaved only after secretion from
the cells by proteolytic enzymes. Pro-collagens are fibrillar
molecules which are lot more (about a thousand fold) stable
than the collagen fibrils. Cleaving of pro-collagens to collagens
inside the cell can lead to catastrophic consequences.
Collagen is the most abundant protein of the extracellular
matrix (ECM). ECM is an intricate network of macromolecules
filling the extracellular space inside the tissues. Other than
collagens, ECM is rich in proteoglycans, glycoproteins and
proteases [5]. In vertebrates, the main function of ECM is to
serve as a scaffold to stabilize the physical structure of tissues.
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