The extracellular matrix of <i>Gadus morhua</i> muscle contains types III, V, VI and IV collagens in addition to type I

Brüggemann, Dagmar; Lawson, Moira A.

doi:10.1111/j.0022-1112.2005.00650.x

Cited by 18 publications

(17 citation statements)

References 28 publications

(20 reference statements)

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“…Collagen I was previously reported to be a major collagen of fish muscle, along with collagen V [26,27]. In our study collagen I epitopes were expressed throughout the ECM in a similar manner as lumican.…”

Section: Discussionsupporting

confidence: 70%

Lumican is a major small leucine-rich proteoglycan (SLRP) in Atlantic cod (Gadus morhua L.) skeletal muscle

et al. 2011

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Knowledge on fish matrix biology is important to ensure optimal fish -quality, -growth and -health in aquaculture. The aquaculture industry face major challenges related to matrix biology, such as inflammations and malformations. Atlantic cod skeletal muscle was investigated for collagen I, decorin, biglycan, and lumican expression and distribution by real-time PCR, immunohistochemical staining and Western blotting. Immunohistochemical staining and Western immunoblotting were also performed using antibodies against glycosaminoglycan side chains of these proteoglycans, in addition to fibromodulin. Real-time PCR showed highest mRNA expression of lumican and collagen I. Collagen I and proteoglycan immunohistochemical staining revealed distinct thread-like structures in the myocommata, with the exception of fibromodulin, which stained in dense structures embedded in the myocommata. Chondroitinase AC-generated epitopes stained more limited than cABC-generated epitopes, indicating a stronger presence of dermatan sulfate than chondroitin sulfate in cod muscle. Lumican and keratan sulfate distribution patterns were strong and ubiquitous in endomysia and myocommata. Western blots revealed similar SLRPs sizes in cod as are known from mammals. Staining of chondroitin/dermatan sulfate epitopes in Western blots were similar in molecular size to those of decorin and biglycan, whereas staining of keratan sulfate epitopes coincided with expected molecular sizes of lumican and fibromodulin. In conclusion, lumican was a major proteoglycan in cod muscle with ubiquitous distribution overlapping with keratan sulfate. Other leucine-rich proteoglycans were also present in cod muscle, and Western blot using antibodies developed for mammalian species showed cross reactivity with fish, demonstrating similar structures and molecular weights as in mammals.

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Section: Discussionsupporting

confidence: 70%

Lumican is a major small leucine-rich proteoglycan (SLRP) in Atlantic cod (Gadus morhua L.) skeletal muscle

et al. 2011

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“…The pure components, collagen I and C‐4‐S, are chosen because other studies have shown that collagen I is the main collagen in the connective tissue in fish and C‐4‐S is the most prominent GAG present in the connective tissue in cod . The FTIR second derivative spectrum of commercial pure component collagen type I shows the strongest bands at amide I (1585‐1720 cm −1 ) and amide II (1500‐1586 cm −1 ) (Figure ).…”

Section: Resultsmentioning

confidence: 99%

“…Several types of collagen are the main constituents of connective tissue and they all contain a characteristic three polypeptide chain, which forms into a unique triple helical structure . Collagen determines the connective tissue strength and structure , and the most abundant collagen type in fish muscle is the fibrillar collagen type I . PGs are complex and multifunctional molecules consisting of a protein core with a variable number of covalently attached carbohydrate side chains, the glycosaminoglycans (GAGs) .…”

Section: Introductionmentioning

confidence: 99%

The use of Fourier‐transform infrared spectroscopy to characterize connective tissue components in skeletal muscle of Atlantic cod (Gadus morhua L.)

Sanden

Köhler

Afseth

et al. 2019

Journal of Biophotonics

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In the present study, Fourier‐transform infrared spectroscopy (FTIR) is investigated as a method to measure connective tissue components that are important for the quality of Atlantic cod filets (Gadus morhua L.). The Atlantic cod used in this study originated from a feeding trial, which found that fish fed a high starch diet contained relative more collagen type I, while fish fed a low starch (LS) diet contained relative more glycosaminoglycans (GAGs) in the connective tissue. FTIR spectra of pure commercial collagen type I and GAGs were acquired to identify spectral markers and compare them with FTIR spectra and images from connective tissue. Using principal component analysis, high and LS diets were separated due to collagen type I in the spectral region 1800 to 800 cm−1. The spatial distribution of collagen type I and GAGs were further investigated by FTIR imaging in combination with immunohistochemistry. Pixel‐wise correlation images were calculated between preprocessed connective tissue images and preprocessed pure components spectra of collagen type I and GAGs, respectively. For collagen, the FTIR images reveal a collagen distribution that closely resembles the collagen distribution as imaged by immunohistochemistry. For GAGs, the concentration is very low. Still, the FTIR images detect the most GAGs rich regions.

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“…Collagen, the main protein of the connective tissue is partly soluble in neutral salt solutions and swells at concentrations <1 M (Brüggemann & Lawson, 2005;Komsa-Penkova, Koynova, Kostov, & Tenchov, 1996;Russell, 1973;Winkler, 1973). Moreover, studies on cattle collagen show that the maximum solubility (Neklyudov, Berdutina, Ivankin, Mitaleva, & Evstaf'eva, 2003) is obtained at similar levels (0.8 M) as for myofibrillar proteins (Stefansson & Hultin, 1994).…”

Section: Introductionmentioning

confidence: 99%

The effects of salt-curing and salting procedures on the microstructure of cod (Gadus morhua) muscle

Þórarinsdóttir¹,

Arason²,

Sigurgísladóttir³

et al. 2011

Food Chemistry

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The extracellular matrix of Gadus morhua muscle contains types III, V, VI and IV collagens in addition to type I

Cited by 18 publications

References 28 publications

Lumican is a major small leucine-rich proteoglycan (SLRP) in Atlantic cod (Gadus morhua L.) skeletal muscle

Lumican is a major small leucine-rich proteoglycan (SLRP) in Atlantic cod (Gadus morhua L.) skeletal muscle

The use of Fourier‐transform infrared spectroscopy to characterize connective tissue components in skeletal muscle of Atlantic cod (Gadus morhua L.)

The effects of salt-curing and salting procedures on the microstructure of cod (Gadus morhua) muscle

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