Collagen and collagenolytic proteases: A review

Bhagwat, Prashant; Dandge, Padma B.

doi:10.1016/j.bcab.2018.05.005

Cited by 78 publications

(35 citation statements)

References 141 publications

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“…The transcriptome or RNA expression levels in these organisms are also being explored with the goal of understanding the timing of transcription, translation, and protein secretion as it pertains to the events occurring in the biomineralizing matrix . What has emerged from these studies…”

Section: Biomineral‐associated Secretomesmentioning

confidence: 99%

“…Other activation and inhibition signaling communicator proteins, such as TGF‐β, fibronectin, thrombospondin, and bone morphogenic proteins are also present in the bone extracellular matrix and participate in bone formation and remodeling as well . The formation of bone tissue is a dynamic ongoing process, and specific proteases, such as cathepsins, collagenase, matrix metalloproteinases, or Cys‐based proteases act as remodelers and degrade matrix proteins, either to allow further volume for mineral expansion, to turn over proteins in preparation for their replacement during bone remodeling or fracture repair processes, to generate polypeptide fragments that act as communicators, or to terminate the mineralization process itself …”

Section: Biomineral‐associated Secretomesmentioning

confidence: 99%

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The Biomineralization Proteome: Protein Complexity for a Complex Bioceramic Assembly Process

Evans

2019

Proteomics

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There are over 62 different biominerals on Earth and a diverse array of organisms that generate these biominerals for survival. This review will introduce the process of biomineralization and the current understanding of the molecular mechanisms of mineral formation, and then comparatively explore the representative secretomes of two well-documented skeletal systems: vertebrate bone (calcium phosphate) and invertebrate mollusk shell (calcium carbonate). It is found that both skeletal secretomes have gross similarities and possess proteins that fall into four functional categories: matrix formers, nucleation assisters, communicators, and remodelers. In many cases the mineral-associated matrix former and nucleation assister sequences in both skeletal systems are unique and possess interactive conserved globular domains, intrinsic disorder, post-translational modifications, sequence redundancy, and amyloid-like aggregation-prone sequences. Together, these molecular features create a protein-based environment that facilitates mineral formation and organization and argue in favor of conserved features that evolve from the mollusk shell to bone. Interestingly, the mollusk shell secretome appears to be more complex compared to that of bone tissue, in that there are numerous protein subcategories that are required for the nucleation and organization of inner (nacre) and outer (prismatic) calcium carbonate regions of the shell. This may reflect the organizational and material requirements of an exoskeletal protective system.

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Section: Biomineral‐associated Secretomesmentioning

confidence: 99%

Section: Biomineral‐associated Secretomesmentioning

confidence: 99%

The Biomineralization Proteome: Protein Complexity for a Complex Bioceramic Assembly Process

Evans

2019

Proteomics

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“…Among those studies, triple-helical “Madras Model” by Ramachandran and Kartha [ 24 ] contributed much to the currently accepted structure of collagen which was discovered by Cowan, North and Randall [ 25 ]. Further findings of Rich and Crick [ 26 ] also improved the identified structure of collagen [ 27 ]. Currently, more than 29 distinct types of collagen have been identified [ 28 , 29 ].…”

Section: Definition and History Of Collagenmentioning

confidence: 99%

“…This technique is often used for fractionation and quantification of proteins in connection with either mass spectrometric identification or immunological test [ 199 ]. Even though SDS-PAGE method is used as a tool to characterize proteins according to their size, charge, relative hydrophobicity and abundance with the newly emerging techniques such as protein sequencing, amino acid compositional analysis, peptide profiling hinders the use of SDS-PAGE for analytical purposes [ 27 , 199 ]. Table 6 summarizes the studies conducted using different sea cucumber species to determine the subunit composition of isolated collagen.…”

Section: Pre-treatment Extraction Isolation and Purificationmentioning

confidence: 99%

Sea Cucumber Derived Type I Collagen: A Comprehensive Review

2020

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Collagen is the major fibrillar protein in most living organisms. Among the different types of collagen, type I collagen is the most abundant one in tissues of marine invertebrates. Due to the health-related risk factors and religious constraints, use of mammalian derived collagen has been limited. This triggers the search for alternative sources of collagen for both food and non-food applications. In this regard, numerous studies have been conducted on maximizing the utilization of seafood processing by-products and address the need for collagen. However, less attention has been given to marine invertebrates and their by-products. The present review has focused on identifying sea cucumber as a potential source of collagen and discusses the general scope of collagen extraction, isolation, characterization, and physicochemical properties along with opportunities and challenges for utilizing marine-derived collagen.

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“…The collagenase used in this study is a protease that can destroy collagen. Due to the triple helix structure, collagen in resistant to many proteases, but collagenase can easily destroy collagen by specific action 1 …”

Section: Forewordmentioning

confidence: 99%