Comparison of the two different phosphagen systems in the lugworm Arenicola marina

Kamp, Günter; Englisch, H.; Müller, R. F.; Westhoff, Dunja; Elsing, A.

doi:10.1007/bf00261305

Cited by 5 publications

(3 citation statements)

References 37 publications

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“…Secondly, polychaete CK3 migrates towards the cathode in cellulose acetate electrophoresis indicating that this protein has a p I greater than pH 8. Kamp et al [15]also observed that the CK from the polychaete Arenicola marina sperm mitochondrial fractions had a p I of 7.9. Vertebrate MiCKs typically have similarly high p I s [1], giving the protein a net positive charge under physiological pH values which may facilitate binding to the outer portion of the inner mitochondrial membrane [1].…”

Section: Discussionmentioning

confidence: 98%

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Origin of octameric creatine kinases

Ellington¹,

Roux²,

Pineda³

1998

FEBS Letters

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Mitochondrial creatine kinase (MiCK) occurs primarily as an octameric form localized in the mitochondrial intermembrane compartment in vertebrate tissues and echinoderm spermatozoa (both deuterostome groups). The octameric quaternary structure is thought to play important functional and enzyme targeting roles. We have found that the spermatozoa of the protostome polychaete Chaetopterus variopedatus contain three distinct isoenzymes of creatine kinase (CK) termed CK1, CK2 and CK3. CK3 appears to be present only in the sperm head/midpiece complex where mitochondria are restricted and has a subunit relative molecular mass (M r ) of 43.4 kDa. Gel permeation chromatography using Superdex 200HR showed that CK3 has a native M r of 344.9 kDa indicating that this enzyme exists as an octamer. Electron micrographs of negatively stained CK3 preparations show structures which are virtually identical to those that have been seen for octameric vertebrate MiCK. The above observations show that CK3 from C. variopedatus displays great similarities to MiCKs from vertebrates and echinoderms. Octamerization of CK is not an advanced feature. The evolution of octameric subunit association is ancient and occurred prior to the divergence of protostomes and deuterostomes.z 1998 Federation of European Biochemical Societies.

show abstract

Section: Discussionmentioning

confidence: 98%

“…However, regardless of which phosphagen kinase is found in the somatic tissues, spermatozoa always have CK only [14]. Recently, Kamp et al [15]found two isoenzymes of CK in the sperm of the polychaete Arenicola marina , a head/midpiece form and a flagellar form. The subunit structure was not characterized.…”

Section: Introductionmentioning

confidence: 99%

Origin of octameric creatine kinases

Ellington¹,

Roux²,

Pineda³

1998

FEBS Letters

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show abstract

“…Even though other phosphagen systems may be present in somatic tissues and eggs, the spermatozoa of all echinoderms, tunicates, and polychaetes consistently have the CP/CK system only (Watts, 1971;Tombs and Shapiro, 1989;Kamp et al, 1995), with CK activities ranging from 7.1 to 30 /umoles * min-1 * mg protein-1 in echinoderms (Ratto et al, 1989). Even though other phosphagen systems may be present in somatic tissues and eggs, the spermatozoa of all echinoderms, tunicates, and polychaetes consistently have the CP/CK system only (Watts, 1971;Tombs and Shapiro, 1989;Kamp et al, 1995), with CK activities ranging from 7.1 to 30 /umoles * min-1 * mg protein-1 in echinoderms (Ratto et al, 1989).…”

Section: Diffusion Of Phosphagens In Physiological Contextmentioning

confidence: 99%

Functional and Evolutionary Implications of the Distribution of Phosphagens in Primitive-Type Spermatozoa

Ellington

Kinsey

1998

The Biological Bulletin

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External fertilization is considered to be the primitive condition in metazoans. The spermatozoa of such organisms typically display a common primitive-type morphology that is present in a range of phyla. These spermatozoa are extremely polarized cells in that the site of ATP synthesis (mitochondria in midpiece) is located at large diffusion distances from the ATP sink (dynein ATPases in the flagellum). Spermatozoa of polychaetes, sipunculids, echiuroids, echinoderms, and tunicates contain the phosphagen creatine phosphate or express the corresponding phosphagen kinase creatine kinase (or both), even when other phosphagens/phosphagen kinases are present in somatic tissues and eggs. The selective expression of the creatine kinase system in these spermatozoa may be related to potential advantages in the cellular transport of energy. To evaluate this possibility, we compared the efficacy of the major phosphagen systems for cellular transport of energy. We used a facilitated diffusion model for spatial ATP buffering, taking into account relative differences in diffusivity and thermodynamic poise. At low ratios of [total phosphagen pool]/ [total adenine nucleotide pool] (CG+P/CAd ratio), creatine phosphate carried a higher fraction of total high-energy phosphate (J) than the other phosphagens. However, J values for all phosphagens were greater than 0.9, and these differences disappeared as the CG+P/CAd ratio was increased. Thus, the functional benefit of using CP, rather than other phosphagens, in energy transport is quite limited. The creatine kinase system became associated with primitive-type spermatozoa early in metazoan evolution. This association is not necessarily related to inherent advantages of this phosphagen system for buffering of ATP, but may be linked to historical events in the evolution of the cell phenotype.

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The capacity for the de novo biosynthesis of creatine is present in the tunicate Ciona intestinalis and is likely widespread in other protochordate and invertebrate groups

DeLigio

Ellington

2006

Comparative Biochemistry and Physiology Part D: Genomics and Pr

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Comparison of the two different phosphagen systems in the lugworm Arenicola marina

Cited by 5 publications

References 37 publications

Origin of octameric creatine kinases

Origin of octameric creatine kinases

Functional and Evolutionary Implications of the Distribution of Phosphagens in Primitive-Type Spermatozoa

The capacity for the de novo biosynthesis of creatine is present in the tunicate Ciona intestinalis and is likely widespread in other protochordate and invertebrate groups

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