416
Recently, collagen-based porous, three-dimensional scaffolds have been widely
used for regenerative medicine and especially for tissue engineering (Lu et al. 2010 ;
Ko et al. 2010 ).
Fish collagen is a renewable source of material and has been successfully used
for practical applications in biomedicine and tissue engineering in both pure
(Kanayama et al. 2008 ) and crosslinked forms (Yunoki et al. 2007 ; Nagai et al.
2008 ). Numerous works were dedicated to shark collagens and their comparison
with pig collagens. The results of these comparative studies prepared by Nomura
and co-workers can be summarized as follow:
– “The physicochemical properties of shark type I collagen gel and membrane
were not same as those of pig type I collagen. The denaturation temperature of
shark collagen gel was about 15 °C lower.
– The breaking strength of shark collagen gel was greater, and shark collagen
membrane had a greater mechanical strength and a higher water vapor sorption,”
(Nomura et al. 2000b ).
– “Fibril reconstruction process that is, the nucleation and growth of mixed type I
collagen fi bril from sharks and pigs, progressed faster than that of the individual
collagen species of shark or pig.
– The reconstructed mixed collagen fi bril had a greater resistance to return to solution or melt into gelatin in comparison with the counterpart consisting solely of
shark collagen.
– The denaturation temperature of the mixed collagen gel was about 10 °C higher
than that of shark, and about 5 °C lower than that of pig. The breaking strength
of the mixed collagen gel was tougher than that of pig, but weaker than that of
shark,” (Nomura et al. 2000a ).
Nomura and Kitazume ( 2002 ) also investigated application of shark collagen as
a substrate for zymography as well as a scaffold for cell culture. More detailed,
“fi broblasts were cultured on a gel matrix of shark type I collagen at 30 °C. The
collagen gel had contracted by 4 days of incubation. Individual fi broblasts were
visible against the transparent background of the contracted collagen as long, lean
star-shaped cells. It was showed that the matrix metalloproteinases (MMPs) from
fi broblasts secreted from the medium more easily digested shark gelatin than pig
gelatin. MMP-2, -9, and that of potential form were recognizable in the zymographic gel of shark gelatin,” (Nomura and Kitazume 2002 ).
Fish scales collagen (FSC) was used to manufacture the scaffold for corneal tissue
engineering (Krishnan et al. 2012 ). “The ex vivo cultured limbal stem cells over a
biocompatible scaffold are used in the management of limbal stem cell defi ciency as
an ideal replacement for human amniotic membrane (HAM). It is important that the
mechanical and physical strengths of FSC were comparable to that of HAM’s. Under
microscopic observation, epithelial migration was noted at the end of 48 h from limbal explants plated on FSC; and after 72 h on HAM. By the end of the 15th day,
90–100 % confl uent growth resembling the morphological features of limbal
epithelium was seen. FSCs were optically clear with suffi cient strength, and gave
13 Marine Structural Proteins in Biomedicine and Tissue Engineering
Recently, collagen-based porous, three-dimensional scaffolds have been widely
used for regenerative medicine and especially for tissue engineering (Lu et al. 2010 ;
Ko et al. 2010 ).
Fish collagen is a renewable source of material and has been successfully used
for practical applications in biomedicine and tissue engineering in both pure
(Kanayama et al. 2008 ) and crosslinked forms (Yunoki et al. 2007 ; Nagai et al.
2008 ). Numerous works were dedicated to shark collagens and their comparison
with pig collagens. The results of these comparative studies prepared by Nomura
and co-workers can be summarized as follow:
– “The physicochemical properties of shark type I collagen gel and membrane
were not same as those of pig type I collagen. The denaturation temperature of
shark collagen gel was about 15 °C lower.
– The breaking strength of shark collagen gel was greater, and shark collagen
membrane had a greater mechanical strength and a higher water vapor sorption,”
(Nomura et al. 2000b ).
– “Fibril reconstruction process that is, the nucleation and growth of mixed type I
collagen fi bril from sharks and pigs, progressed faster than that of the individual
collagen species of shark or pig.
– The reconstructed mixed collagen fi bril had a greater resistance to return to solution or melt into gelatin in comparison with the counterpart consisting solely of
shark collagen.
– The denaturation temperature of the mixed collagen gel was about 10 °C higher
than that of shark, and about 5 °C lower than that of pig. The breaking strength
of the mixed collagen gel was tougher than that of pig, but weaker than that of
shark,” (Nomura et al. 2000a ).
Nomura and Kitazume ( 2002 ) also investigated application of shark collagen as
a substrate for zymography as well as a scaffold for cell culture. More detailed,
“fi broblasts were cultured on a gel matrix of shark type I collagen at 30 °C. The
collagen gel had contracted by 4 days of incubation. Individual fi broblasts were
visible against the transparent background of the contracted collagen as long, lean
star-shaped cells. It was showed that the matrix metalloproteinases (MMPs) from
fi broblasts secreted from the medium more easily digested shark gelatin than pig
gelatin. MMP-2, -9, and that of potential form were recognizable in the zymographic gel of shark gelatin,” (Nomura and Kitazume 2002 ).
Fish scales collagen (FSC) was used to manufacture the scaffold for corneal tissue
engineering (Krishnan et al. 2012 ). “The ex vivo cultured limbal stem cells over a
biocompatible scaffold are used in the management of limbal stem cell defi ciency as
an ideal replacement for human amniotic membrane (HAM). It is important that the
mechanical and physical strengths of FSC were comparable to that of HAM’s. Under
microscopic observation, epithelial migration was noted at the end of 48 h from limbal explants plated on FSC; and after 72 h on HAM. By the end of the 15th day,
90–100 % confl uent growth resembling the morphological features of limbal
epithelium was seen. FSCs were optically clear with suffi cient strength, and gave
13 Marine Structural Proteins in Biomedicine and Tissue Engineering