Collagen family of proteins

Rest, Michel van der; Garrone, R.

doi:10.1096/fasebj.5.13.1916105

Cited by 1,098 publications

(591 citation statements)

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“…More than 90% of the dry weight of the ECM from most tissues and organs consists of collagen. 17 The main subtypes that make up the lung's structure are collagens I, III, IV, and V. Type I collagen is the major structural protein present in tissues. In nature, collagen is closely associated with glycosylated proteins, growth factors and other structural proteins such as elastin and laminin, which provide unique tissue properties.…”

Section: Discussionmentioning

confidence: 99%

Sodium hydroxide based non-detergent decellularizing solution for rat lung

et al. 2018

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Lung transplantation is the last option for the treatment of end stage chronic lung disorders. Because the shortage of donor lung organs represents the main hurdle, lung regeneration has been considered to overcome this hurdle. Recellularization of decellularized organ scaffold is a promising option for organ regeneration. Although detergents are ordinarily used for decellularization, other approaches are possible. Here we used high alkaline (pH12) sodium hydroxide (NaOH)-PBS solution without detergents for lung decellularization and compared the efficacy on DNA elimination and ECM preservation with detergent based decellularization solutions CHAPS and SDS. Immunohistochemical image analysis showed that cell components were removed by NaOH solution as well as other detergents. A Collagen and GAG assay showed that the collagen reduction of the NaOH group was comparable to that of the CHAPS and SDS groups. However, DNA reduction was more significant in the NaOH group than in other groups (p < 0.0001). The recellularization of HUVEC revealed cell attachment was not inferior to that of the SDS group. Ex vivo functional analysis showed 100% oxygen ventilation increased oxygen partial pressure as artificial hemoglobin vesicle-PBS solution passed through regenerated lungs in the SDS or NaOH group. It was concluded that the NaOH-PBS based decellularization solution was comparable to ordinal decellularizaton solutions and competitive in cost effectiveness and residues in the decellularized scaffold negligible, thus providing another potential option to detergent for future clinical usage.

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Section: Discussionmentioning

confidence: 99%

Sodium hydroxide based non-detergent decellularizing solution for rat lung

et al. 2018

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“…In normal skin, collagen types I and VI are localized diffusely throughout the dermis and collagen VI also shows a pronounced reactivity close to basement membranes [18]. Both collagen types are basically important to maintain regular structural functions [2,8,12].…”

Section: Discussionmentioning

confidence: 99%

“…Up to now 14 different collagen subtypes have been identified, 6 of which can be localized in human skin [18]. The use of the immunohistochemical detection of collagen types I, III and IV for a forensically applicable wound age-determination has previously been shown by Eisenmenger et al [7], while studies dealing with the time-dependent appearance of collagen types III, IV, V and VII have been performed by Betz et al [3,4,5].…”

Section: Introductionmentioning

confidence: 99%

Immunohistochemical localization of collagen types I and VI in human skin wounds

Betz

Nerlich²,

Wilske

et al. 1993

Int J Leg Med

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Summary.A total of 74 human skin wounds were investigated and collagen types I and VI were localized in the wound area by immunohistochemistry. Collagen type I appeared in the form of ramifying string-like structures after approximately 5-6 days, but positive reactions in the form of a spot-like staining around isolated fibroblasts also occurred in a skin wound aged 4 days. Collagen VI was detectable after a post-infliction interval of at least 3 days showing a strongly positive reacting network associated with fibroblasts in the wound area. Both collagens appeared almost constantly after a wound age of 6-7 days and could also be found in wounds aged a few months. Therefore, although a positive reaction for collagen type I in the form of string-like and ramifying structures around wound fibroblasts indicates a wound age of at least 5-6 days, a spot-like positive staining for collagen type I cannot exclude a wound age of at least 4 days. A positive staining for collagen type VI represents a postinfliction time of 3 days or more. The almost constant appearance of these collagen types suggests that negative results in a sufficient number of specimens indicate a wound age of less than 6-7 days, but cannot completely exclude longer post-infliction intervals. Since collagen type I and VI are also found in the granulation/scar tissue of lesions with advanced wound age, the immunohistochemical analysis of these proteins provides no further information for an age determination of older skin wounds.

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“…To this end, we isolated overlapping cDNAs coding for the mouse polypeptide and localized the corresponding transcripts in the developing mouse embryo by in situ Collagen molecules provide physiological and biomechanical properties to most tissues and organs, in addition to participating in several cellular activities and morphogenetic programs (Hay, 1991). Based on common characteristics, the numerous vertebrate collagen types are segregated into several related groups, the largest of which includes the fibril-forming collagens (types I, 11, 111, V, and XI) (Vuorio and de Crombrugghe, 1990;van der Rest and Garrone, 1991). Depending on their relative representation, the fibrillar "minor" types (Burgeson, 1988).…”

Section: Introductionmentioning

confidence: 99%

Localization of pro‐α2(V) collagen transcripts in the tissues of the developing mouse embryo

Ανδρικόπουλος

Suzuki

Solursh

et al. 1992

Developmental Dynamics

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Correct assembly of fibrillar collagen networks plays a critical role in animal morphogenesis. Very little is known about the contribution of the so-called minor fibrillar collagens (types V and XI) to fibrillogenesis. Here we examined the developmental expression of the mouse pro-a2(V) collagen gene (~0 1 5~2 )after the cloning and sequencing of cDNAs that cover the entire length of the message. Transcripts of co15a2, detectable as early as 9 days of gestation, localize with distinct patterns in the tissues of day 12.5 and day 16.5 fetuses. The earlier developmental stage is characterized by low and diffuse coZ5a2 expression in the peritoneal membranes and intestinal and craniofacial mesenchymes. The later stage exhibits higher and more restricted coZ5a2 mRNA accumulation in primary ossified regions, perichondrium, joints, tendon, atrioventricular valve of the heart, and selected portions of the head. A parallel analysis using a cartilagespecific pro-al(I1) collagen (coZ2al) probe confirmed that these two collagen genes are transcribed in a mutually exclusive manner during mouse embryogenesis. On the other hand, the developmental pattern of coZ5a2 expression closely resembles that of the type I collagen, thus further substantiating the notion that these macromolecules cooperate in the formation of fibrillar networks in non-cartilaginous matrices. 0 1992 Wiley-Liss, Inc.

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Collagen family of proteins

Cited by 1,098 publications

References 4 publications

Sodium hydroxide based non-detergent decellularizing solution for rat lung

Sodium hydroxide based non-detergent decellularizing solution for rat lung

Immunohistochemical localization of collagen types I and VI in human skin wounds

Localization of pro‐α2(V) collagen transcripts in the tissues of the developing mouse embryo

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