Structure and immune expression analysis of hemoglobin genes from the blood clam Tegillarca granosa

Bao, Yongbo; Wang, Q.; Zhang, Lin

doi:10.4238/2013.february.28.5

Cited by 17 publications

(14 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…compared to the control groups. Differential temporal expression patterns of T. granosa HbII-A and -B genes in hemocytes were also detected in the presence of microbial ligands (LPS and PGN) and intact bacteria [140, 141]. Over 20 individual nucleotide polymorphisms have been identified across all three T. granosa Hb genes [141].…”

Section: An Emerging Role For Invertebrate (Bivalve) Hemoglobin In Inmentioning

confidence: 99%

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

Coates

Decker

2016

Cell. Mol. Life Sci.

123

View full text Add to dashboard Cite

It is now well documented that peptides with enhanced or alternative functionality (termed cryptides) can be liberated from larger, and sometimes inactive, proteins. A primary example of this phenomenon is the oxygen-transport protein hemoglobin. Aside from respiration, hemoglobin and hemoglobin-derived peptides have been associated with immune modulation, hematopoiesis, signal transduction and microbicidal activities in metazoans. Likewise, the functional equivalents to hemoglobin in invertebrates, namely hemocyanin and hemerythrin, act as potent immune effectors under certain physiological conditions. The purpose of this review is to evaluate the true extent of oxygen-transport protein dynamics in innate immunity, and to impress upon the reader the multi-functionality of these ancient proteins on the basis of their structures. In this context, erythrocyte–pathogen antibiosis and the immune competences of various erythroid cells are compared across diverse taxa.Electronic supplementary materialThe online version of this article (doi:10.1007/s00018-016-2326-7) contains supplementary material, which is available to authorized users.

show abstract

Section: An Emerging Role For Invertebrate (Bivalve) Hemoglobin In Inmentioning

confidence: 99%

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

Coates

Decker

2016

Cell. Mol. Life Sci.

123

View full text Add to dashboard Cite

show abstract

“…), a bivalve mollusk from the Arcidae family, is widely distributed on China’s east coast and in Southeast Asia [10]. It is a major fishery and aquaculture species with proteins, various vitamins and amino acids, resulting in its use in traditional Chinese medicine and seafood [11].…”

Section: Introductionmentioning

confidence: 99%

Purification and Partial Characterization of a New Antitumor Protein from Tegillarca granosa

Gao

Liu

et al. 2015

Marine Drugs

View full text Add to dashboard Cite

A new protein, coded as D2-3, was obtained from the marine organism Tegillarca granosa L. by anion exchange and hydrophobic chromatography. The purity of D2-3 was over 99.0% as measured by RP-HPLC. Its molecular weight was shown to be 20.320 kDa by ESI-MS/MS, and the isoelectric point of D2-3 was 4.70. The antitumor activity of D2-3 against four human tumor cell lines was measured by MTT assay. The conformational structure of D2-3 was further characterized by UV-vis, FT-IR and CD spectroscopy. Partial amino acid sequences of D2-3 were determined to be LMMTDVEESR, SSHMLSECRRK, KNGRNVDISHKDKG, SSDPTLMDPDDTNKDR, SSDKNTCSKTEYYTR and SSETMPYDVLDTNEMR via MALDI-TOF-MS and de novo sequencing.

show abstract

“…This sequencing has demonstrated that the majority of species examined most frequently have two to three Hb encoding genes. For example, Tegillarca granosa contains three different Hb genes; α and β encoding genes of the tetrameric Hb and a minor globin gene encoding the homo-dimeric Hb (Bao et al, 2013a). S.inaequivalvis also expresses three homologous Hb genes (α, β and minor) (Piro et al, 1996;Piro et al, 1998).…”

Section: Haemoglobins In the Family Arcidae Pteriomorphia Subclassmentioning

confidence: 99%

“…It is now widely accepted that invertebrate Hbs are understudied, particularly in reference to their evolution, distribution and functions (Alyakrinskaya, 2002;Bao et al, 2013a). In an attempt to address this knowledge gap, a quantitative investigation of Hb encoding genes was performed across five different tissues in A. trapezia individuals undergoing aerial exposure.…”

Section: Tissue Specific Expression and Neofunctionalisationmentioning

confidence: 99%

“…Haemoglobins (Hbs) are among the best studied proteins in vertebrates but little is known about their distribution, function and evolution in invertebrate lineages (Alyakrinskaya, 2002;Bao et al, 2013a). A number of invertebrate lineages have independently evolved circulating Hbs as a mechanism to transport O 2 for cellular respiration (Mangum et al, 1975).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Characterisation of Duplicated Haemoglobin Genes in Bivalves

Klein¹

View full text Add to dashboard Cite

Haemoglobins (Hbs) are found in virtually all phyla and are some of the most investigated proteins in biomedical sciences. These proteins exhibit an extraordinary diversity of form and function in invertebrate lineages. This provides a unique opportunity to explore the origin and evolution of Hbs yet little is known about their distribution, function and evolution in invertebrate lineages. To explore further the functions and evolution of those Hbs, recent transcriptome data for the Arcid bivalve Anadara trapezia is investigated here. This species shows the presence of duplicated Hb encoding genes suggesting that gene duplication may have been more extensive than previously thought in bivalves. This study tests the hypothesis that these duplicated genes show patterns of tissue specific expression and evidence of neofunctionalisation. This is shown here for at least three Hb encoding genes present in A. trapezia with strong tissue specific expression in haemolymph compared to other tissues. Furthermore, the expression of these genes remains unaffected by prolonged air exposure suggesting that neofunctionalisation may confer an evolutionary advantage to this bivalve. As well as the unique Hbs found in the bivalve order Arcoida, Hbs are also found in three other bivalve orders: Carditoida, Solemyoida and Veneroida. These four orders that possess Hbs provide compelling evidence for the independent evolution of these proteins in multiple bivalve lineages.To expand data on the distribution of Hbs in bivalves, a transcriptome sequence for Ctenoides ales in the order Limoida was generated in this project. Interrogation of the transcriptome shows the presence of at least three globin-like encoding genes including two Hb-like encoding genes providing preliminary evidence for another independent origin of Hb in a bivalve lineage. Overall, this study provides novel insights into the function, evolution and distribution of Hbs in bivalves by investigating two distantly related species. Results of this study are consistent with current theories that Hb diversity in bivalves is a result of repeated rounds of gene duplication providing the raw material for evolution. Investigation of hypoxic resistance also reinforces that greater expression of Hbs in haemolymph confers a physiological advantage suggesting that Hb would evolve more often in some lineages during adaptation to unfavourable environment conditions, particularlyAbstract ii hypoxia and prolonged air exposure.The finding of Hb-like encoding genes in another bivalve lineage also supports the evolution of this gene family through independent evolution and gene duplication, and gives insight into the distribution of globin genes in bivalves which is still poorly understood. The investigation of Hb genes in these bivalves also contributes to further understand the role of Hbs and provides potential novel insights for resistance in hypoxic environments, disease control and resistance to pollution in aquaculture.Abstract iii

show abstract

Structure and immune expression analysis of hemoglobin genes from the blood clam Tegillarca granosa

Cited by 17 publications

References 30 publications

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

Purification and Partial Characterization of a New Antitumor Protein from Tegillarca granosa

Characterisation of Duplicated Haemoglobin Genes in Bivalves

Contact Info

Product

Resources

About