Diabetes

Poor glycemic control linked to sarcopenia in T2DM

(HealthDay)—For patients with type 2 diabetes, poor glycemic control is associated with sarcopenia, according to a study published online May 9 in the Journal of Diabetes Investigation.

Medications

Medication nonadherence common in patients with T2DM

(HealthDay)—Routine urine samples can be used to test for medication adherence in patients with type 2 diabetes, according to a study published in the June issue of Diabetes Care.

Diabetes

Dapagliflozin improves glucose outcomes in type 1 diabetes

(HealthDay)—In patients with type 1 diabetes, treatment with dapagliflozin for 24 weeks improves time in range, mean glucose, and glycemic variability, according to a study published online April 9 in Diabetes Care.

Diabetes

Achievement of targets in T2DM varies by season

(HealthDay)—There is seasonal variation in achievement of the guideline targets for hemoglobin A1c (HbA1c), blood pressure (BP), and low-density lipoprotein (LDL) cholesterol among persons with type 2 diabetes mellitus ...

Diabetes

Rates of diabetes screening high among adults age <45

(HealthDay)—Rates of diabetes screening are high, with hemoglobin A1c (HbA1c) used less but more likely to result in clinical diagnosis, according to a study published online Feb. 6 in Diabetes Care.

Diabetes

Investigators study effect of switching insulin medications

In the United States, the drug price for insulin has skyrocketed over the last two decades. While the price has increased for all forms of insulin, newer, "analogue" insulin medications such as glargine and lispro have become ...

Health

Short duration between dinner, bed has no effect on HbA1c

(HealthDay)—Ensuring a short duration between dinner and bedtime has no effect on hemoglobin A1c (HbA1c) levels in middle-aged and older Japanese adults, according to a study published online Jan. 22 in BMJ Nutrition, Prevention ...

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.

page 1 from 23

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.

This text uses material from Wikipedia, licensed under CC BY-SA