2006
DOI: 10.1016/j.biomaterials.2006.07.035
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Stability, sterility, coagulation, and immunologic studies of salmon coagulation proteins with potential use for mammalian wound healing and cell engineering

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Cited by 22 publications
(39 citation statements)
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“…The differences between salmon and mammalian fibrin may be attributed to species-specific variations in the fibrinogen sequence. Fibrinogen is a large glycoprotein containing pairs of three subunit chains Aα, Bβ, and γ. Fibrinogen chains are heavily glycosylated, and differences in carbohydrate modifications between salmon and mammalian fibrinogens may underlie some of the discrepancies between species, including variations in charge and solubility [20,24]. The salmon genome has recently been sequenced and comparison of the predicted amino acid sequences of salmon and mammalian (human and bovine) fibrinogen reveals discrepancies in the location of RGD sequences within the chains.…”
Section: Discussionmentioning
confidence: 99%
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“…The differences between salmon and mammalian fibrin may be attributed to species-specific variations in the fibrinogen sequence. Fibrinogen is a large glycoprotein containing pairs of three subunit chains Aα, Bβ, and γ. Fibrinogen chains are heavily glycosylated, and differences in carbohydrate modifications between salmon and mammalian fibrinogens may underlie some of the discrepancies between species, including variations in charge and solubility [20,24]. The salmon genome has recently been sequenced and comparison of the predicted amino acid sequences of salmon and mammalian (human and bovine) fibrinogen reveals discrepancies in the location of RGD sequences within the chains.…”
Section: Discussionmentioning
confidence: 99%
“…Salmon fibrin matches the mechanical characteristics of CNS tissue [20,22] and when used to treat rats with dorsal hemisection spinal cord injuries promotes greater locomotor functional recovery, density of serotonergic fibers caudal to the lesion site, and recovery of bladder function than mammalian fibrin [23]. Salmon fibrin has been developed as a human therapeutic and has passed numerous toxicity and immunogenicity tests [24,25]. Although salmon fibrin is an effective scaffold to treat CNS injury [23], it degrades rapidly in vivo (~7 days) and thus is unlikely to provide long-term support for transplanted hNSPCs.…”
Section: Introductionmentioning
confidence: 99%
“…Intraperitoneal injections of salmon fibrin in both rats and rabbits resulted in no negative effects regarding coagulation or cross-reactivity. After repeated administration of salmon fibrin, animals produced antibodies against the salmon proteins, but did not produce antibodies that cross-reacted with host proteins [33, 46]. Also, there was no effect in coagulation tests, a result that was also found in studies of swine that had been treated with salmon fibrin [47, 48].…”
Section: Discussionmentioning
confidence: 99%
“…Compared to mammalian fibrin, salmon fibrin promotes more neurite growth, shows a slower degradation profile, and is non-toxic in animal models [26]. Further, salmon fibrin clots readily at temperatures as low as 0°C, while human fibrinogen activated by thrombin clots slowly below 23°C [33]; this difference provides an advantage in situations where hypothermia must be used. A swine aortotomy model demonstrated salmon fibrin dressing to be effective in controlling severe bleeding [34].…”
Section: Introductionmentioning
confidence: 99%
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