378
Chronology of these experimental works is excellently represented in the work by
Rouse and Van Dyke ( 2010 ) as follow:
“In 1934, a key research paper was published that described different types of
keratins, distinguished primarily by having different molecular weights. This seminal
paper demonstrated that there were many different keratin derivatives, and that each
played a different role in the structure and function of the hair follicle. […] In 1965,
CSIRO scientist W. Gordon Crewther and his colleagues published the defi nitive
text on the chemistry of keratins. This chapter in Advances in Protein Chemistry
contained references to more than 640 published studies on keratins. […] Advances
in the extraction, purifi cation and characterization of keratins, led to the exponential
growth of keratin materials and their derivatives. In the 1970s, methods to form
extracted keratins into powders, fi lms, gels, coatings, fi bers, and foams were developed and published by several research groups. All of these methods made use of
the oxidative and reductive chemistries developed decades earlier, or variations
thereof,” (Rouse and Van Dyke 2010 ; see also Crewther et al. 1965 ; Goddard and
Michaelis 1935 ).
Systematization of knowledge on structure, function and regulation of mammalian keratins synthesis led to their classifi cation of these structural proteins into two
distinct groups (see for review Block 1951 ; Langbein et al. 1999 , 2001 ; Schweizer
et al. 2006 ). According to Rouse and Van Dyke ( 2010 ), “‘Hard’ keratins form
ordered arrays of IFs embedded in a matrix of cystine rich proteins and contribute
to the tough structure of epidermal appendages. ‘Soft’ keratins preferentially form
loosely-packed bundles of cytoplasmic IFs and endow mechanical resilience to
epithelial cells. In 2006, Schweizer et al. developed a new consensus nomenclature
for hard and soft keratins to accommodate the functional genes and pseudogenes for
the full complement of human keratins. The structural subunits of both epithelial
and hair keratins are two chains of differing molecular weight and composition
(designated types I and II). They each contain non-helical end terminal domains and
a highly-conserved, central alpha-helical domain.
The type I (acidic) and type II (neutral-basic) keratin chains interact to form
heterodimers, which in turn further polymerize to form 10-nm intermediate fi laments,” (Rouse and Van Dyke 2010 ).
After 30 years keratin research, the total number of mammalian keratins has
increased to 54, including 28 type I and 26 type II keratins (Karantza 2011 ).
Chemistry of mammalian keratins (Crewther et al. 1965 ), their composition, structure and biosynthesis (Dobb and Rogers 1967 ; Fraser et al. 1972 ), biology and
pathology (Moll et al. 2008 ), functions (Kirfel et al. 2003 ; Gu and Coulombe 2007 ;
Magin et al. 2007 ), genetics (Hesse et al. 2001 ), mechanical (Yamada et al. 2003 ) and
material properties (Hill et al. 2010 ; Rouse and Van Dyke 2010 ) are well studied.
“Recently, keratins have been recognized as regulators of numerous cellular properties and functions. These include apico-basal polarization, motility, cell size, protein
synthesis, membrane traffi cking, and signalling. In cancer, keratins are extensively
used as diagnostic tumor markers. Epithelial malignancies largely maintain the specifi c keratin patterns associated with their respective cells of origin, and, in many
occasions, full-length or cleaved keratin expression (or lack thereof) in tumors and/
11 Marine Keratins
Chronology of these experimental works is excellently represented in the work by
Rouse and Van Dyke ( 2010 ) as follow:
“In 1934, a key research paper was published that described different types of
keratins, distinguished primarily by having different molecular weights. This seminal
paper demonstrated that there were many different keratin derivatives, and that each
played a different role in the structure and function of the hair follicle. […] In 1965,
CSIRO scientist W. Gordon Crewther and his colleagues published the defi nitive
text on the chemistry of keratins. This chapter in Advances in Protein Chemistry
contained references to more than 640 published studies on keratins. […] Advances
in the extraction, purifi cation and characterization of keratins, led to the exponential
growth of keratin materials and their derivatives. In the 1970s, methods to form
extracted keratins into powders, fi lms, gels, coatings, fi bers, and foams were developed and published by several research groups. All of these methods made use of
the oxidative and reductive chemistries developed decades earlier, or variations
thereof,” (Rouse and Van Dyke 2010 ; see also Crewther et al. 1965 ; Goddard and
Michaelis 1935 ).
Systematization of knowledge on structure, function and regulation of mammalian keratins synthesis led to their classifi cation of these structural proteins into two
distinct groups (see for review Block 1951 ; Langbein et al. 1999 , 2001 ; Schweizer
et al. 2006 ). According to Rouse and Van Dyke ( 2010 ), “‘Hard’ keratins form
ordered arrays of IFs embedded in a matrix of cystine rich proteins and contribute
to the tough structure of epidermal appendages. ‘Soft’ keratins preferentially form
loosely-packed bundles of cytoplasmic IFs and endow mechanical resilience to
epithelial cells. In 2006, Schweizer et al. developed a new consensus nomenclature
for hard and soft keratins to accommodate the functional genes and pseudogenes for
the full complement of human keratins. The structural subunits of both epithelial
and hair keratins are two chains of differing molecular weight and composition
(designated types I and II). They each contain non-helical end terminal domains and
a highly-conserved, central alpha-helical domain.
The type I (acidic) and type II (neutral-basic) keratin chains interact to form
heterodimers, which in turn further polymerize to form 10-nm intermediate fi laments,” (Rouse and Van Dyke 2010 ).
After 30 years keratin research, the total number of mammalian keratins has
increased to 54, including 28 type I and 26 type II keratins (Karantza 2011 ).
Chemistry of mammalian keratins (Crewther et al. 1965 ), their composition, structure and biosynthesis (Dobb and Rogers 1967 ; Fraser et al. 1972 ), biology and
pathology (Moll et al. 2008 ), functions (Kirfel et al. 2003 ; Gu and Coulombe 2007 ;
Magin et al. 2007 ), genetics (Hesse et al. 2001 ), mechanical (Yamada et al. 2003 ) and
material properties (Hill et al. 2010 ; Rouse and Van Dyke 2010 ) are well studied.
“Recently, keratins have been recognized as regulators of numerous cellular properties and functions. These include apico-basal polarization, motility, cell size, protein
synthesis, membrane traffi cking, and signalling. In cancer, keratins are extensively
used as diagnostic tumor markers. Epithelial malignancies largely maintain the specifi c keratin patterns associated with their respective cells of origin, and, in many
occasions, full-length or cleaved keratin expression (or lack thereof) in tumors and/
11 Marine Keratins