361
© Springer Science+Business Media Dordrecht 2015
H. Ehrlich, Biological Materials of Marine Origin, Biologically- Inspired Systems 4,
DOI 10.1007/978-94-007-5730-1_10
Chapter 10
Marine Elastin
Abstract Elastic function for a lifetime in animals, including marine vertebrates is
determined by the structural protein elastin. Extracellular matrix is the space where
a monomer, tropoelastin, is rapidly transformed into its fi nal polymeric form.
Desmosine and isodesmosine serve as crosslinking molecules, binding the polymeric chains of amino acids into the 3D network of elastin. Elastin is located within
such tissues and organs as skin, arteria, heart, notochord and swimbladder in marine
fi sh. Interestingly, the lamprey possesses only elastin-like fi brillar proteins. The whale
heart and aorta are the largest elastin-containing structures known in Nature.
According to defi nition, proposed by Miao et al. ( 2006 ), “elastin is the extracellular
matrix protein responsible for properties of extensibility and elastic recoil in large
blood vessels, lung, and skin of most vertebrates,” (Miao et al. 2006 ). In 1963,
Partridge and co-workers reported in Nature the fi rst isolation of two new amino
acids, named desmosine and isodesmosine, from the elastin of bovine ligamentum
nuchae (Partridge et al. 1963 ). Further studies by Thomas et al. ( 1963 ) showed these
compounds to be 1,3,4,5- and 1,2,3,5-tetra-substituted pyridinium salts, with each
side chain having both a carboxyl-terminal and -amino terminal group. The side
chain at position 1 was found to be a B-carbon straight chain. These amino acids
seem to be essential components of elastin, and have been shown to be present in
elastins obtained from various sources (Anwar 1966 ; Kielty et al. 2002 ). They serve
as crosslinking molecules, binding the polymeric chains of amino acids into the 3D
network of elastin (Piez 1968 ). Unique type of amino acid derived from the condensation of four lysine residues is known as desmosine (including the isomer isodesmosine) (Fig. 10.1 ) (see for review Anwar and Oda 1966 ; Partridge 1966 ; Petruska
and Sandberg 1968 ; Franzblau and Lent 1968 ; Shimada et al. 1969 ). “This unique
characteristic is considered useful in discriminating elastin breakdown-derived peptides from precursor elastin peptides. Based on this feature, desmosine has been
extensively evaluated as a potentially attractive indicator of elevated lung elastic
fi bre turnover, and a marker for the effectiveness of agents with the potential to
reduce elastin breakdown,” (Luisetti et al. 2012 ; see for more information Turino
et al. 2011 ).
Since the very fi rst publications on elastin chemistry (Partridge et al. 1955 ),
structure ( Greenlee et al. 1966 ) and isolation in the chemically pure form (Steven
et al. 1974 ; Starcher and Galione 1976 ; Soskel et al. 1987 ), numerous papers were
© Springer Science+Business Media Dordrecht 2015
H. Ehrlich, Biological Materials of Marine Origin, Biologically- Inspired Systems 4,
DOI 10.1007/978-94-007-5730-1_10
Chapter 10
Marine Elastin
Abstract Elastic function for a lifetime in animals, including marine vertebrates is
determined by the structural protein elastin. Extracellular matrix is the space where
a monomer, tropoelastin, is rapidly transformed into its fi nal polymeric form.
Desmosine and isodesmosine serve as crosslinking molecules, binding the polymeric chains of amino acids into the 3D network of elastin. Elastin is located within
such tissues and organs as skin, arteria, heart, notochord and swimbladder in marine
fi sh. Interestingly, the lamprey possesses only elastin-like fi brillar proteins. The whale
heart and aorta are the largest elastin-containing structures known in Nature.
According to defi nition, proposed by Miao et al. ( 2006 ), “elastin is the extracellular
matrix protein responsible for properties of extensibility and elastic recoil in large
blood vessels, lung, and skin of most vertebrates,” (Miao et al. 2006 ). In 1963,
Partridge and co-workers reported in Nature the fi rst isolation of two new amino
acids, named desmosine and isodesmosine, from the elastin of bovine ligamentum
nuchae (Partridge et al. 1963 ). Further studies by Thomas et al. ( 1963 ) showed these
compounds to be 1,3,4,5- and 1,2,3,5-tetra-substituted pyridinium salts, with each
side chain having both a carboxyl-terminal and -amino terminal group. The side
chain at position 1 was found to be a B-carbon straight chain. These amino acids
seem to be essential components of elastin, and have been shown to be present in
elastins obtained from various sources (Anwar 1966 ; Kielty et al. 2002 ). They serve
as crosslinking molecules, binding the polymeric chains of amino acids into the 3D
network of elastin (Piez 1968 ). Unique type of amino acid derived from the condensation of four lysine residues is known as desmosine (including the isomer isodesmosine) (Fig. 10.1 ) (see for review Anwar and Oda 1966 ; Partridge 1966 ; Petruska
and Sandberg 1968 ; Franzblau and Lent 1968 ; Shimada et al. 1969 ). “This unique
characteristic is considered useful in discriminating elastin breakdown-derived peptides from precursor elastin peptides. Based on this feature, desmosine has been
extensively evaluated as a potentially attractive indicator of elevated lung elastic
fi bre turnover, and a marker for the effectiveness of agents with the potential to
reduce elastin breakdown,” (Luisetti et al. 2012 ; see for more information Turino
et al. 2011 ).
Since the very fi rst publications on elastin chemistry (Partridge et al. 1955 ),
structure ( Greenlee et al. 1966 ) and isolation in the chemically pure form (Steven
et al. 1974 ; Starcher and Galione 1976 ; Soskel et al. 1987 ), numerous papers were