After care
After a dislocation, injured joints are usually held in place by a splint (for straight joints like fingers and toes) or a bandage (for complex joints like shoulders). Additionally, the joint muscles, tendons and ligaments must also be strengthened. This is usually done through a course of physiotherapy, which will also help reduce the chances of repeated dislocations of the same joint.For glenohumeral instability, the therapeutic program depends on specific characteristics of the instability pattern, severity, recurrence and direction with adaptations made based on the needs of the patient. In general, the therapeutic program should focus on restoration of strength, normalization of range of motion and optimization of flexibility and muscular performance. Throughout all stages of the rehabilitation program, it is important to take all related joints and structures into consideration. Epidemiology
Each joint in the body can be dislocated, however, there are common sites where most dislocations occur. The following structures are the most common sites of joint dislocations:
Dislocated shoulder
Shoulder dislocations account for 45% of all dislocation visits to the emergency room. Anterior shoulder dislocation, the most common type of shoulder dislocation (96-98% of the time) occurs when the arm is in external rotation and abduction (away from the body) produces a force that displaces the humeral head anteriorly and downwardly. Vessel and nerve injuries during a shoulder dislocation is rare, but can cause many impairments and requires a longer recovery process.
Together with folate, cobalamins are essential cofactors required for DNA synthesis in cells where chromosomal replication and division are occurring—most notably the bone marrow and myeloid cells. As a cofactor, cobalamins are essential for two cellular reactions:

the mitochondrial methylmalonyl-CoA mutase conversion of methylmalonic acid (MMA) to succinate, which links lipid and carbohydrate metabolism, and
the activation of methionine synthase, which is the rate-limiting step in the synthesis of methionine from homocysteine and 5-methyltetrahydrofolate.Cobalamins are characterized by a porphyrin-like corrin nucleus that contains a single cobalt atom bound to a benzimidazolyl nucleotide and a variable residue (R) group. The variable R group gives rise to the four most commonly known cobalamins: CNCbl, methylcobalamin, 5-deoxyadenosylcobalamin, and OHCbl. In the serum, hydroxocobalamin and cyanocobalamin are believed to function as storage or transport forms of the molecule, whereas methylcobalamin and 5-deoxyadenosylcobalamin are the active forms of the coenzyme required for cell growth and replication. Cyanocobalamin is usually converted to hydroxocobalamin in the serum, whereas hydroxocobalamin is converted to either methylcobalamin or 5-deoxyadenosyl cobalamin. Cobalamins circulate bound to serum proteins called transcobalamins (TC) and haptocorrins. Hydroxocobalamin has a higher affinity to the TC II transport protein than cyanocobalamin, or 5-deoxyadenosylcobalamin. From a biochemical point of view, two essential enzymatic reactions require vitamin B12 (cobalamin).Intracellular vitamin B12 is maintained in two active coenzymes, methylcobalamin and 5-deoxyadenosylcobalamin. In the face of vitamin B12 deficiency, conversion of methylmalonyl-CoA to succinyl-CoA cannot take place, which results in accumulation of methylmalonyl-CoA and aberrant fatty acid synthesis.