Diabetes

Long work hours tied to poor glycemic control in T2DM

(HealthDay)—Long work hours (≥60 hours/week) are associated with poor glycemic control in young Japanese men with type 2 diabetes, according to a study published in the January issue of the Journal of Diabetes Investigation.

Medical research

No bleeding required: Anemia detection via smartphone

Biomedical engineers have developed a smartphone app for the non-invasive detection of anemia. Instead of a blood test, the app uses photos of someone's fingernails taken on a smartphone to accurately measure how much hemoglobin ...

Diabetes

Basal insulin analogues similar for glucose lowering

(HealthDay)—Basal insulin analogues for type 2 diabetes mellitus (T2DM) do not substantially differ in their glucose-lowering effect, according to a review published online July 10 in the Annals of Internal Medicine.

Diabetes

Two regimens fail to stop declines in β-cell function

(HealthDay)—Neither glargine followed by metformin nor metformin alone halts the progressive deterioration of β-cell function in youth with impaired glucose tolerance (IGT) or recently-diagnosed type 2 diabetes, according ...

Diabetes

HbA1c targets should be personalized in type 2 diabetes

(HealthDay)—For non-pregnant adults with type 2 diabetes, hemoglobin A1c (HbA1c) targets should be personalized, according to a Clinical Guidelines Synopsis published in the June 19 issue of the Journal of the American ...

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Hemoglobin

Hemoglobin (English pronunciation: /hiːməˈɡloʊbɪn/; also rendered as haemoglobin and abbreviated Hb or Hgb) is the iron-containing oxygen-transport metalloprotein in the red blood cells of all vertebrates, with the exception of the fish family Channichthyidae, as well as the tissues of some invertebrates. Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the rest of the body (i.e., the tissues) where it releases the oxygen to burn nutrients to provide energy to power the functions of the organism, and collects the resultant carbon dioxide to bring it back to the respiratory organs to be dispensed from the organism.

In mammals, the protein makes up about 97% of the red blood cells' dry content, and around 35% of the total content (including water).[citation needed] Hemoglobin has an oxygen binding capacity of 1.34 ml O2 per gram of hemoglobin, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood. The mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules.

Hemoglobin is involved in the transport of other gases: it carries some of the body's respiratory carbon dioxide (about 10% of the total) as carbaminohemoglobin, in which CO2 is bound to the globin protein. The molecule also carries the important regulatory molecule nitric oxide bound to a globin protein thiol group, releasing it at the same time as oxygen.

Hemoglobin is also found outside red blood cells and their progenitor lines. Other cells that contain hemoglobin include the A9 dopaminergic neurons in the substantia nigra, macrophages, alveolar cells, and mesangial cells in the kidney. In these tissues, hemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism.

Hemoglobin and hemoglobin-like molecules are also found in many invertebrates, fungi, and plants. In these organisms, hemoglobins may carry oxygen, or they may act to transport and regulate other things such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. A variant of the molecule, called leghemoglobin, is used to scavenge oxygen, to keep it from poisoning anaerobic systems, such as nitrogen-fixing nodules of leguminous plants.

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