Hemoglobin D: Difference between revisions
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'''Hemoglobin D''' ('''HbD''') is a [[Hemoglobin variants|variant of hemoglobin]], a protein complex that makes up [[red blood cells]]. Based on the locations of the original identification, it has been known by several names such as '''hemoglobin D-Los Angeles''', '''hemoglobin D-Punjab''',<ref name=":0">{{Cite journal |last1=Torres |first1=Lidiane de Souza |last2=Okumura |first2=Jéssika Viviani |last3=Silva |first3=Danilo Grünig Humberto da |last4=Bonini-Domingos |first4=Claudia Regina |date=March 2015 |title=Hemoglobin D-Punjab: origin, distribution and laboratory diagnosis |journal=Revista Brasileira de Hematologia e Hemoterapia |language=en |volume=37 |issue=2 |pages=120–126 |doi=10.1016/j.bjhh.2015.02.007 |issn=1516-8484 |pmc=4382585 |pmid=25818823 |doi-access=free}}</ref> '''D-North Carolina''', '''D-Portugal''', '''D-Oak Ridge''', and '''D-Chicago.<ref name=":1">{{Cite journal |last1=El-Kalla |first1=S. |last2=Mathews |first2=A. R. |date=January 1997 |title=HB D-Punjab in the United Arab Emirates |url=http://dx.doi.org/10.3109/03630269709000669 |journal=Hemoglobin |volume=21 |issue=4 |pages=369–375 |doi=10.3109/03630269709000669 |issn=0363-0269 |pmid=9255615}}</ref>''' Hemoglobin D-Los Angeles was the first type identified by [[Harvey Itano]] in 1951, and was subsequently discovered that hemoglobin D-Punjab is the most abundant type that is common in Sikh people of Punjab (of both Pakistan and India) and of Gujarat.<ref>{{Cite journal |last=Shekhda |first=Kalyan Mansukhbhai |date=2017 |title=Co-Inheritance of Haemoglobin D-Punjab and Beta Thalassemia - A Rare Variant |url=http://jcdr.net/article_fulltext.asp?issn=0973-709x&year=2017&volume=11&issue=6&page=OD21&issn=0973-709x&id=10114 |journal=Journal of Clinical and Diagnostic Research |volume=11 |issue=6 |pages=21–22 |doi=10.7860/JCDR/2017/27816.10114 |pmc=5535424 |pmid=28764232}}</ref> Unlike normal adult human hemoglobin ([[Hemoglobin A|HbA]]) which has [[glutamic acid]] at its 121 amino acid position, it has [[glutamine]] instead.<ref name=":2">{{Citation |last=Randolph |first=Tim R. |title=Hemoglobinopathies (structural defects in hemoglobin) |date=2020 |work=Rodak's Hematology |pages=394–423 |url=https://linkinghub.elsevier.com/retrieve/pii/B9780323530453000337 |access-date=2024-02-29 |publisher=Elsevier |language=en |doi=10.1016/b978-0-323-53045-3.00033-7 |isbn=978-0-323-53045-3}}</ref> The single amino acid substitution can cause various [[blood diseases]], from fatal genetic anemia to mild [[hemolytic anemia]], an abnormal destruction of red blood cells.<ref>{{Cite journal |last=Shanthala Devi |first=A. M. |last2=Rameshkumar |first2=Karuna |last3=Sitalakshmi |first3=S. |date=2016 |title=Hb D: A Not So Rare Hemoglobinopathy |url=https://link.springer.com/article/10.1007/s12288-013-0319-3 |journal=Indian Journal of Hematology & Blood Transfusion: An Official Journal of Indian Society of Hematology and Blood Transfusion |volume=32 |issue=Suppl 1 |pages=294–298 |doi=10.1007/s12288-013-0319-3 |issn=0971-4502 |pmc=4925467 |pmid=27408416}}</ref> Depending on the type of genetic inheritance, it can produce four different conditions: h.<ref name=":2" /> heterozygous (inherited in only one of the chromosome 11) HbD trait, HbD-thalassemia, HbS-D (sickle cell) disease, and, very rarely, homozygous (inherited in both chromosome 11) HbD disease.<ref>{{Citation |last=Dasgupta |first=Amitava |title=Hemoglobinopathy |date=2014 |work=Clinical Chemistry, Immunology and Laboratory Quality Control |pages=363–390 |url=https://linkinghub.elsevier.com/retrieve/pii/B9780124078215000218 |access-date=2024-02-29 |publisher=Elsevier |language=en |doi=10.1016/b978-0-12-407821-5.00021-8 |isbn=978-0-12-407821-5 |last2=Wahed |first2=Amer}}</ref> |
'''Hemoglobin D''' ('''HbD''') is a [[Hemoglobin variants|variant of hemoglobin]], a protein complex that makes up [[red blood cells]]. Based on the locations of the original identification, it has been known by several names such as '''hemoglobin D-Los Angeles''', '''hemoglobin D-Punjab''',<ref name=":0">{{Cite journal |last1=Torres |first1=Lidiane de Souza |last2=Okumura |first2=Jéssika Viviani |last3=Silva |first3=Danilo Grünig Humberto da |last4=Bonini-Domingos |first4=Claudia Regina |date=March 2015 |title=Hemoglobin D-Punjab: origin, distribution and laboratory diagnosis |journal=Revista Brasileira de Hematologia e Hemoterapia |language=en |volume=37 |issue=2 |pages=120–126 |doi=10.1016/j.bjhh.2015.02.007 |issn=1516-8484 |pmc=4382585 |pmid=25818823 |doi-access=free}}</ref> '''D-North Carolina''', '''D-Portugal''', '''D-Oak Ridge''', and '''D-Chicago.<ref name=":1">{{Cite journal |last1=El-Kalla |first1=S. |last2=Mathews |first2=A. R. |date=January 1997 |title=HB D-Punjab in the United Arab Emirates |url=http://dx.doi.org/10.3109/03630269709000669 |journal=Hemoglobin |volume=21 |issue=4 |pages=369–375 |doi=10.3109/03630269709000669 |issn=0363-0269 |pmid=9255615}}</ref>''' Hemoglobin D-Los Angeles was the first type identified by [[Harvey Itano]] in 1951, and was subsequently discovered that hemoglobin D-Punjab is the most abundant type that is common in Sikh people of Punjab (of both Pakistan and India) and of Gujarat.<ref>{{Cite journal |last=Shekhda |first=Kalyan Mansukhbhai |date=2017 |title=Co-Inheritance of Haemoglobin D-Punjab and Beta Thalassemia - A Rare Variant |url=http://jcdr.net/article_fulltext.asp?issn=0973-709x&year=2017&volume=11&issue=6&page=OD21&issn=0973-709x&id=10114 |journal=Journal of Clinical and Diagnostic Research |volume=11 |issue=6 |pages=21–22 |doi=10.7860/JCDR/2017/27816.10114 |pmc=5535424 |pmid=28764232}}</ref> Unlike normal adult human hemoglobin ([[Hemoglobin A|HbA]]) which has [[glutamic acid]] at its 121 amino acid position, it has [[glutamine]] instead.<ref name=":2">{{Citation |last=Randolph |first=Tim R. |title=Hemoglobinopathies (structural defects in hemoglobin) |date=2020 |work=Rodak's Hematology |pages=394–423 |url=https://linkinghub.elsevier.com/retrieve/pii/B9780323530453000337 |access-date=2024-02-29 |publisher=Elsevier |language=en |doi=10.1016/b978-0-323-53045-3.00033-7 |isbn=978-0-323-53045-3}}</ref> The single amino acid substitution can cause various [[blood diseases]], from fatal genetic anemia to mild [[hemolytic anemia]], an abnormal destruction of red blood cells.<ref>{{Cite journal |last=Shanthala Devi |first=A. M. |last2=Rameshkumar |first2=Karuna |last3=Sitalakshmi |first3=S. |date=2016 |title=Hb D: A Not So Rare Hemoglobinopathy |url=https://link.springer.com/article/10.1007/s12288-013-0319-3 |journal=Indian Journal of Hematology & Blood Transfusion: An Official Journal of Indian Society of Hematology and Blood Transfusion |volume=32 |issue=Suppl 1 |pages=294–298 |doi=10.1007/s12288-013-0319-3 |issn=0971-4502 |pmc=4925467 |pmid=27408416}}</ref> Depending on the type of genetic inheritance, it can produce four different conditions: h.<ref name=":2" /> heterozygous (inherited in only one of the chromosome 11) HbD trait, HbD-thalassemia, HbS-D (sickle cell) disease, and, very rarely, homozygous (inherited in both chromosome 11) HbD disease.<ref>{{Citation |last=Dasgupta |first=Amitava |title=Hemoglobinopathy |date=2014 |work=Clinical Chemistry, Immunology and Laboratory Quality Control |pages=363–390 |url=https://linkinghub.elsevier.com/retrieve/pii/B9780124078215000218 |access-date=2024-02-29 |publisher=Elsevier |language=en |doi=10.1016/b978-0-12-407821-5.00021-8 |isbn=978-0-12-407821-5 |last2=Wahed |first2=Amer}}</ref> |
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== Structure == |
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Hemoglobin D has the basic structure and composition of normal adult hemoglobin. It is a globular protein containing [[Prosthetic group|prosthetic]] (non-protein) group called heme. There are four individual peptide chains, namely two α- and two β-subunits, each made of 141 and 146 amino acid residues, respectively. One heme is associated with each chain and responsible for binding free oxygen in the blood. A single HbD is therefore a [[Tetrameric protein|tetramer]] (containing four molecules), denoted as α<sub>2</sub>β<sub>2</sub>.<ref>{{Cite journal |last=Ahmed |first=Mostafa H. |last2=Ghatge |first2=Mohini S. |last3=Safo |first3=Martin K. |date=2020 |title=Hemoglobin: Structure, Function and Allostery |url=https://link.springer.com/chapter/10.1007/978-3-030-41769-7_14 |journal=Sub-Cellular Biochemistry |volume=94 |pages=345–382 |doi=10.1007/978-3-030-41769-7_14 |issn=0306-0225 |pmc=7370311 |pmid=32189307}}</ref> Each subunit has a molecular weight of about 16,000 Da ([[Dalton (unit)|daltons]]), making the tetramer about 64,000 Da (64,458 g/mol) in size.<ref>{{Cite journal |last=Palmer |first=Andre F. |last2=Sun |first2=Guoyong |last3=Harris |first3=David R. |date=2009 |title=Tangential flow filtration of hemoglobin |url=https://aiche.onlinelibrary.wiley.com/doi/10.1002/btpr.119 |journal=Biotechnology Progress |volume=25 |issue=1 |pages=189–199 |doi=10.1002/btpr.119 |issn=1520-6033 |pmc=2647581 |pmid=19224583}}</ref> HbD is different from HbA only on the β-subunit where the amino acid glutamic acid at 121 amino acid position is replaced with glutamine.<ref name=":2" /> |
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== References == |
== References == |
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* [https://www.britannica.com/science/celiac-disease Disease information in Encyclopædia Britannica] |
* [https://www.britannica.com/science/celiac-disease Disease information in Encyclopædia Britannica] |
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* [https://www.healthy.arkansas.gov/images/uploads/hemoglobin_d_trait.pdf Fact sheet] |
* [https://www.healthy.arkansas.gov/images/uploads/hemoglobin_d_trait.pdf Fact sheet] |
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{{Hemeproteins}}{{Medical resources|DiseasesDB=29718|ICD10={{ICD10|D|58|2|d|55}}|ICD9={{ICD9|282.7}}|ICDO=|OMIM=|MedlinePlus=|eMedicineSubj=|eMedicineTopic=|MeshID=C032001}} |
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{{Hemeproteins}} |
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[[Category:Hemoglobins]] |
[[Category:Hemoglobins]] |
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[[Category:Respiratory physiology]] |
[[Category:Respiratory physiology]] |
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Revision as of 07:35, 29 February 2024
Hemoglobin D (HbD) is a variant of hemoglobin, a protein complex that makes up red blood cells. Based on the locations of the original identification, it has been known by several names such as hemoglobin D-Los Angeles, hemoglobin D-Punjab,[1] D-North Carolina, D-Portugal, D-Oak Ridge, and D-Chicago.[2] Hemoglobin D-Los Angeles was the first type identified by Harvey Itano in 1951, and was subsequently discovered that hemoglobin D-Punjab is the most abundant type that is common in Sikh people of Punjab (of both Pakistan and India) and of Gujarat.[3] Unlike normal adult human hemoglobin (HbA) which has glutamic acid at its 121 amino acid position, it has glutamine instead.[4] The single amino acid substitution can cause various blood diseases, from fatal genetic anemia to mild hemolytic anemia, an abnormal destruction of red blood cells.[5] Depending on the type of genetic inheritance, it can produce four different conditions: h.[4] heterozygous (inherited in only one of the chromosome 11) HbD trait, HbD-thalassemia, HbS-D (sickle cell) disease, and, very rarely, homozygous (inherited in both chromosome 11) HbD disease.[6]
Structure
Hemoglobin D has the basic structure and composition of normal adult hemoglobin. It is a globular protein containing prosthetic (non-protein) group called heme. There are four individual peptide chains, namely two α- and two β-subunits, each made of 141 and 146 amino acid residues, respectively. One heme is associated with each chain and responsible for binding free oxygen in the blood. A single HbD is therefore a tetramer (containing four molecules), denoted as α2β2.[7] Each subunit has a molecular weight of about 16,000 Da (daltons), making the tetramer about 64,000 Da (64,458 g/mol) in size.[8] HbD is different from HbA only on the β-subunit where the amino acid glutamic acid at 121 amino acid position is replaced with glutamine.[4]
References
- ^ Torres, Lidiane de Souza; Okumura, Jéssika Viviani; Silva, Danilo Grünig Humberto da; Bonini-Domingos, Claudia Regina (March 2015). "Hemoglobin D-Punjab: origin, distribution and laboratory diagnosis". Revista Brasileira de Hematologia e Hemoterapia. 37 (2): 120–126. doi:10.1016/j.bjhh.2015.02.007. ISSN 1516-8484. PMC 4382585. PMID 25818823.
- ^ El-Kalla, S.; Mathews, A. R. (January 1997). "HB D-Punjab in the United Arab Emirates". Hemoglobin. 21 (4): 369–375. doi:10.3109/03630269709000669. ISSN 0363-0269. PMID 9255615.
- ^ Shekhda, Kalyan Mansukhbhai (2017). "Co-Inheritance of Haemoglobin D-Punjab and Beta Thalassemia - A Rare Variant". Journal of Clinical and Diagnostic Research. 11 (6): 21–22. doi:10.7860/JCDR/2017/27816.10114. PMC 5535424. PMID 28764232.
- ^ a b c Randolph, Tim R. (2020), "Hemoglobinopathies (structural defects in hemoglobin)", Rodak's Hematology, Elsevier, pp. 394–423, doi:10.1016/b978-0-323-53045-3.00033-7, ISBN 978-0-323-53045-3, retrieved 2024-02-29
- ^ Shanthala Devi, A. M.; Rameshkumar, Karuna; Sitalakshmi, S. (2016). "Hb D: A Not So Rare Hemoglobinopathy". Indian Journal of Hematology & Blood Transfusion: An Official Journal of Indian Society of Hematology and Blood Transfusion. 32 (Suppl 1): 294–298. doi:10.1007/s12288-013-0319-3. ISSN 0971-4502. PMC 4925467. PMID 27408416.
- ^ Dasgupta, Amitava; Wahed, Amer (2014), "Hemoglobinopathy", Clinical Chemistry, Immunology and Laboratory Quality Control, Elsevier, pp. 363–390, doi:10.1016/b978-0-12-407821-5.00021-8, ISBN 978-0-12-407821-5, retrieved 2024-02-29
- ^ Ahmed, Mostafa H.; Ghatge, Mohini S.; Safo, Martin K. (2020). "Hemoglobin: Structure, Function and Allostery". Sub-Cellular Biochemistry. 94: 345–382. doi:10.1007/978-3-030-41769-7_14. ISSN 0306-0225. PMC 7370311. PMID 32189307.
- ^ Palmer, Andre F.; Sun, Guoyong; Harris, David R. (2009). "Tangential flow filtration of hemoglobin". Biotechnology Progress. 25 (1): 189–199. doi:10.1002/btpr.119. ISSN 1520-6033. PMC 2647581. PMID 19224583.