Evolutionary Aspects of Hemoglobin Scavengers

Abstract

With the evolution of fish, systems appeared for the disposal of the hemoglobin (Hb) that was inevitably released from erythrocytes. Thus, a plasma protein that bound free Hb with great affinity, haptoglobin (Hp), evolved from a protease of the innate immune system. In parallel, other proteins appeared (for example, hemopexin and alpha(1)-microglobulin), which bound and mediated the removal of free heme groups. Remarkably, Hp later disappeared in some vertebrate lineages, suggesting that it could also be disadvantageous. In the avian lineage, a soluble protein evolved, possibly from a scavenger receptor, which in some birds seems to have replaced Hp. Among mammals, multimeric forms of Hp appeared independently at two discrete times, suggesting that this form of the protein confers an advantage on the bearer, possibly by improving resistance to infection.

Measuring of the salivary immunoglobulin in Callithrix jacchus primates in captivity running title: salivary immunoglobulin in marmoset

“…There could even be a negative correlation between these values (Ganhao et al 1984), which generates doubts about the interpretation of the results that use concentration as a parameter (Herbert & Cohen 1993). According to Wicher & Fries (2010), the structure of proteins such as haptoglobulin varies between species, even close ones, probably due to evolution. This structural difference between the molecules could explain the low affinity of salivary IgA from these primates with the antibodies in the kit used.…”

Measuring of the salivary immunoglobulin in Callithrix jacchus primates in captivity running title: salivary immunoglobulin in marmoset

“…There could even be a negative correlation between these values (Ganhao et al 1984), which generates doubts about the interpretation of the results that use concentration as a parameter (Herbert & Cohen 1993). According to Wicher & Fries (2010), the structure of proteins such as haptoglobulin varies between species, even close ones, probably due to evolution. This structural difference between the molecules could explain the low affinity of salivary IgA from these primates with the antibodies in the kit used.…”

Haptoglobin Is a Divergent MASP Family Member That Neofunctionalized To Recycle Hemoglobin via CD163 in Mammals

“…Phylogenetic analysis of Hp and the MASP family revealed the presence of a monophyletic Hp clade in jawed vertebrates that included our cartilaginous fish sequences, with branching patterns matching closely to expected species phylogeny (figure 1c). Critically, unlike previous studies (9, 14), we probabilistically determined the best-fitting amino acid substitution model and incorporated a relaxed molecular clock model to infer the root of the tree (25) as an appropriate outgroup is not known. The root fell between a MASP-1 clade (TCN) and a Hp + AGY-type MASP clade (figure 1c; supplemental figure 2a).…”

The Equine PeptideAtlas: A resource for developing proteomics‐based veterinary research

“…Lavoie‐Lamoureux et al have found that haptoglobin is a marker of both acute and chronic systemic inflammation in equine heave, Pihl et al designated it as a potential marker in peritoneal fluid for inflammatory abdominal conditions, and Wolf et al found that its concentration increased in uterine samples from mares upon endometritis . Haptoglobin is a glycoprotein composed of two α and two β chains . In the Equine PeptideAtlas the sequence coverage is 67.9% and includes a total of 19 observed peptides with EOS ≥ 0.3 only mapping to this protein group, and representing both the α and β chain.…”

Measuring of the salivary immunoglobulin in Callithrix jacchus primates in captivity running title: salivary immunoglobulin in marmoset

“…There could even be a negative correlation between these values (Ganhao et al 1984), which generates doubts about the interpretation of the results that use concentration as a parameter (Herbert & Cohen 1993). According to Wicher & Fries (2010), the structure of proteins such as haptoglobulin varies between species, even close ones, probably due to evolution. This structural difference between the molecules could explain the low affinity of salivary IgA from these primates with the antibodies in the kit used.…”

Haptoglobin Is a Divergent MASP Family Member That Neofunctionalized To Recycle Hemoglobin via CD163 in Mammals

“…Phylogenetic analysis of Hp and the MASP family revealed the presence of a monophyletic Hp clade in jawed vertebrates that included our cartilaginous fish sequences, with branching patterns matching closely to expected species phylogeny (figure 1c). Critically, unlike previous studies (9, 14), we probabilistically determined the best-fitting amino acid substitution model and incorporated a relaxed molecular clock model to infer the root of the tree (25) as an appropriate outgroup is not known. The root fell between a MASP-1 clade (TCN) and a Hp + AGY-type MASP clade (figure 1c; supplemental figure 2a).…”

The Equine PeptideAtlas: A resource for developing proteomics‐based veterinary research

“…Lavoie‐Lamoureux et al have found that haptoglobin is a marker of both acute and chronic systemic inflammation in equine heave, Pihl et al designated it as a potential marker in peritoneal fluid for inflammatory abdominal conditions, and Wolf et al found that its concentration increased in uterine samples from mares upon endometritis . Haptoglobin is a glycoprotein composed of two α and two β chains . In the Equine PeptideAtlas the sequence coverage is 67.9% and includes a total of 19 observed peptides with EOS ≥ 0.3 only mapping to this protein group, and representing both the α and β chain.…”

Measuring of the salivary immunoglobulin in Callithrix jacchus primates in captivity running title: salivary immunoglobulin in marmoset

“…There could even be a negative correlation between these values (Ganhao et al 1984), which generates doubts about the interpretation of the results that use concentration as a parameter (Herbert & Cohen 1993). According to Wicher & Fries (2010), the structure of proteins such as haptoglobulin varies between species, even close ones, probably due to evolution. This structural difference between the molecules could explain the low affinity of salivary IgA from these primates with the antibodies in the kit used.…”

Haptoglobin Is a Divergent MASP Family Member That Neofunctionalized To Recycle Hemoglobin via CD163 in Mammals

“…Phylogenetic analysis of Hp and the MASP family revealed the presence of a monophyletic Hp clade in jawed vertebrates that included our cartilaginous fish sequences, with branching patterns matching closely to expected species phylogeny (figure 1c). Critically, unlike previous studies (9, 14), we probabilistically determined the best-fitting amino acid substitution model and incorporated a relaxed molecular clock model to infer the root of the tree (25) as an appropriate outgroup is not known. The root fell between a MASP-1 clade (TCN) and a Hp + AGY-type MASP clade (figure 1c; supplemental figure 2a).…”

The Equine PeptideAtlas: A resource for developing proteomics‐based veterinary research

“…Lavoie‐Lamoureux et al have found that haptoglobin is a marker of both acute and chronic systemic inflammation in equine heave, Pihl et al designated it as a potential marker in peritoneal fluid for inflammatory abdominal conditions, and Wolf et al found that its concentration increased in uterine samples from mares upon endometritis . Haptoglobin is a glycoprotein composed of two α and two β chains . In the Equine PeptideAtlas the sequence coverage is 67.9% and includes a total of 19 observed peptides with EOS ≥ 0.3 only mapping to this protein group, and representing both the α and β chain.…”